Barium in PDB 9h7z: Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions

Enzymatic activity of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions

Protein crystallography data

Other elements in 9h7z:

Barium Binding Sites:

Barium binding site 1 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 1 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 1 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba618 b:31.1 occ:0.29 H A:VAL560 2.5 33.1 1.0 HA A:HIS559 2.6 36.0 1.0 HG22 A:VAL560 2.8 33.2 1.0 CE1 A:HIS516 2.8 37.1 1.0 HE1 A:HIS516 2.9 44.6 1.0 NE2 A:HIS516 3.1 36.9 1.0 N1 A:FAD606 3.1 25.1 1.0 ND1 A:HIS516 3.2 38.4 1.0 HB3 A:HIS559 3.3 33.9 1.0 N A:VAL560 3.3 27.5 1.0 C10 A:FAD606 3.3 25.7 1.0 HE2 A:HIS516 3.4 44.3 1.0 CA A:HIS559 3.4 29.9 1.0 C2 A:FAD606 3.4 27.0 1.0 H1'1 A:FAD606 3.5 30.6 1.0 HG13 A:VAL560 3.5 38.1 1.0 ND1 A:HIS559 3.6 28.8 1.0 CD2 A:HIS516 3.7 34.7 1.0 CB A:HIS559 3.7 28.2 1.0 CG A:HIS516 3.7 34.8 1.0 CG2 A:VAL560 3.8 27.6 1.0 C4X A:FAD606 3.8 27.5 1.0 N10 A:FAD606 3.8 25.6 1.0 C A:HIS559 3.9 29.0 1.0 N3 A:FAD606 3.9 25.8 1.0 O2 A:FAD606 4.0 27.0 1.0 CG A:HIS559 4.0 28.8 1.0 C4 A:FAD606 4.1 26.3 1.0 C1' A:FAD606 4.1 25.4 1.0 HG21 A:VAL560 4.3 33.2 1.0 CG1 A:VAL560 4.3 31.7 1.0 HD2 A:HIS516 4.3 41.8 1.0 HG23 A:VAL560 4.3 33.2 1.0 H1'2 A:FAD606 4.3 30.6 1.0 CB A:VAL560 4.4 28.8 1.0 HN3 A:FAD606 4.4 31.1 1.0 O A:HOH869 4.4 35.4 1.0 CA A:VAL560 4.4 28.8 1.0 N5 A:FAD606 4.6 27.3 1.0 O A:SER558 4.6 30.2 1.0 C9A A:FAD606 4.6 26.0 1.0 HB3 A:HIS516 4.6 38.6 1.0 HB2 A:HIS559 4.6 33.9 1.0 N A:HIS559 4.6 28.0 1.0 H A:MET561 4.7 31.1 1.0 HG11 A:VAL560 4.7 38.1 1.0 CE1 A:HIS559 4.7 30.1 1.0 O A:HOH859 4.7 30.0 1.0 CB A:HIS516 4.8 32.0 1.0 O A:HOH943 4.8 32.4 1.0 C5X A:FAD606 4.9 26.8 1.0 O4 A:FAD606 5.0 29.2 1.0 HG12 A:VAL560 5.0 38.1 1.0

Barium binding site 2 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 2 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 2 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba619 b:34.7 occ:0.33 H A:GLY346 2.4 41.3 1.0 O A:HOH851 3.1 33.3 1.0 O A:HOH774 3.2 34.5 1.0 HB2 A:GLN345 3.2 43.6 1.0 N A:GLY346 3.3 34.3 1.0 HD2 A:ARG176 3.5 38.0 1.0 HG3 A:GLN347 3.5 36.8 1.0 HB2 A:ALA418 3.5 48.3 1.0 HH11 A:ARG176 3.6 37.0 1.0 HA A:GLN345 3.7 42.8 1.0 CB A:GLN345 4.0 36.3 1.0 CA A:GLY346 4.0 33.0 1.0 OD1 A:ASN66 4.1 31.2 1.0 HD3 A:ARG176 4.1 38.0 1.0 C A:GLY346 4.1 33.2 1.0 HA2 A:GLY346 4.1 39.8 1.0 CA A:GLN345 4.1 35.6 1.0 HG2 A:GLN347 4.2 36.8 1.0 O A:GLY346 4.2 33.2 1.0 C A:GLN345 4.2 35.8 1.0 CD A:ARG176 4.2 31.6 1.0 CG A:GLN347 4.2 30.6 1.0 NH1 A:ARG176 4.3 30.7 1.0 HB3 A:GLN345 4.4 43.6 1.0 CB A:ALA418 4.5 40.2 1.0 HG23 A:THR178 4.5 44.6 1.0 HG21 A:THR178 4.5 44.6 1.0 HB3 A:ALA418 4.6 48.3 1.0 HG1 A:THR417 4.6 41.4 1.0 HH12 A:ARG176 4.7 37.0 1.0 N A:GLN347 4.7 30.6 1.0 H A:THR417 4.7 42.1 1.0 O A:HOH939 4.8 30.0 1.0 H A:GLN347 4.9 36.9 1.0 OE1 A:GLN345 4.9 35.9 1.0 HB1 A:ALA418 4.9 48.3 1.0 HA3 A:GLY346 4.9 39.8 1.0 CD A:GLN347 4.9 30.1 1.0 CG2 A:THR178 5.0 37.0 1.0

Barium binding site 3 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 3 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 3 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba620 b:40.8 occ:0.35 O A:HOH969 2.8 37.3 1.0 HD1 A:PHE160 3.0 44.6 1.0 O A:HOH930 3.0 35.8 1.0 HB2 A:PHE160 3.2 43.6 1.0 ND1 A:HIS158 3.3 33.6 1.0 HD3 A:PRO149 3.3 44.8 1.0 HG3 A:PRO216 3.3 37.8 1.0 HG3 A:PRO175 3.5 40.8 1.0 O A:HOH912 3.5 33.0 1.0 HG3 A:PRO149 3.6 44.1 1.0 HB3 A:HIS158 3.6 42.1 1.0 CD1 A:PHE160 3.8 37.1 1.0 HB3 A:PRO149 3.8 43.3 1.0 HD3 A:PRO216 3.9 36.9 1.0 CE1 A:HIS158 4.0 34.6 1.0 CB A:PHE160 4.1 36.2 1.0 CD A:PRO149 4.1 37.3 1.0 HE1 A:HIS158 4.1 41.6 1.0 CG A:HIS158 4.1 35.7 1.0 CG A:PRO216 4.1 31.4 1.0 CG A:PRO149 4.2 36.7 1.0 HA A:PHE215 4.3 37.4 1.0 N A:PRO216 4.3 30.4 1.0 HA A:PHE160 4.3 42.8 1.0 CD A:PRO216 4.3 30.7 1.0 CB A:HIS158 4.3 35.0 1.0 HA A:PRO216 4.4 35.1 1.0 CG A:PHE160 4.4 35.9 1.0 CG A:PRO175 4.4 33.9 1.0 O A:TYR159 4.4 34.3 1.0 C A:PHE215 4.5 28.7 1.0 CB A:PRO149 4.5 36.0 1.0 H A:TYR159 4.5 40.8 1.0 HB3 A:PRO216 4.6 37.6 1.0 HD3 A:PRO175 4.6 40.4 1.0 CA A:PHE160 4.6 35.6 1.0 C A:TYR159 4.7 34.8 1.0 HD2 A:PRO149 4.7 44.8 1.0 CA A:PRO216 4.7 29.2 1.0 HB3 A:PHE160 4.8 43.6 1.0 CB A:PRO216 4.8 31.3 1.0 CE1 A:PHE160 4.8 36.8 1.0 HE1 A:PHE160 4.8 44.2 1.0 CA A:PHE215 4.8 31.1 1.0 O A:PHE215 4.8 29.5 1.0 HG2 A:PRO175 4.9 40.8 1.0 HG2 A:PRO216 4.9 37.8 1.0 O A:HOH760 4.9 39.2 1.0 N A:PHE160 4.9 35.6 1.0 HA A:HIS158 4.9 41.8 1.0 N A:TYR159 4.9 33.9 1.0 N A:PRO149 4.9 35.8 1.0

Barium binding site 4 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 4 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 4 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba621 b:47.7 occ:0.32 H A:LEU373 2.8 48.6 1.0 HH12 A:ARG400 2.8 60.0 1.0 HB2 A:LEU373 3.0 50.8 1.0 O A:ASN370 3.3 46.6 1.0 HA A:THR371 3.3 48.5 1.0 HG A:LEU373 3.5 52.1 1.0 C A:THR371 3.5 41.2 1.0 N A:LEU373 3.6 40.4 1.0 NH1 A:ARG400 3.6 49.9 1.0 H A:GLU374 3.7 49.5 1.0 O A:THR371 3.7 42.0 1.0 CA A:THR371 3.8 40.3 1.0 C A:ASN370 3.8 45.3 1.0 CB A:LEU373 3.8 42.2 1.0 HD12 A:LEU373 3.9 54.3 1.0 N A:THR371 3.9 42.3 1.0 N A:LYS372 3.9 40.1 1.0 HH11 A:ARG400 4.0 60.0 1.0 CG A:LEU373 4.0 43.4 1.0 HH22 A:ARG400 4.1 60.3 1.0 H A:LYS372 4.1 48.2 1.0 O A:HOH887 4.1 47.1 1.0 CA A:LEU373 4.3 40.5 1.0 N A:GLU374 4.4 41.1 1.0 CD1 A:LEU373 4.5 45.2 1.0 H A:THR371 4.5 50.8 1.0 HB2 A:GLU374 4.5 58.9 1.0 C A:LYS372 4.5 39.2 1.0 CZ A:ARG400 4.6 52.1 1.0 HB3 A:LEU373 4.6 50.8 1.0 NH2 A:ARG400 4.7 50.2 1.0 CA A:LYS372 4.7 38.0 1.0 O A:LEU369 4.7 42.0 1.0 HA A:ASN370 4.7 52.3 1.0 HA A:LYS372 4.8 45.8 1.0 HD11 A:LEU393 4.9 57.8 1.0 CA A:ASN370 4.9 43.5 1.0 C A:LEU373 4.9 41.8 1.0 HD11 A:LEU373 5.0 54.3 1.0

Barium binding site 5 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 5 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 5 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba622 b:45.7 occ:0.29 O A:HOH1024 2.4 47.0 1.0 HB3 A:HIS387 2.7 51.8 1.0 O A:HOH976 2.9 47.8 1.0 HA2 A:GLY529 3.1 42.8 1.0 HG3 A:PRO321 3.2 43.6 1.0 HD2 A:HIS387 3.3 59.9 1.0 HB2 A:ASN388 3.3 50.6 1.0 O A:HOH968 3.5 40.0 1.0 CB A:HIS387 3.6 43.1 1.0 HB3 A:ASN388 3.7 50.6 1.0 HB3 A:PRO321 3.7 42.7 1.0 HA3 A:GLY529 3.8 42.8 1.0 CA A:GLY529 3.8 35.6 1.0 HB2 A:HIS387 3.9 51.8 1.0 CB A:ASN388 4.0 42.1 1.0 CD2 A:HIS387 4.0 49.9 1.0 CG A:PRO321 4.1 36.2 1.0 CG A:HIS387 4.2 47.1 1.0 HD21 A:ASN388 4.2 60.2 1.0 CB A:PRO321 4.3 35.5 1.0 HD3 A:PRO321 4.4 44.1 1.0 N A:ASN388 4.4 40.3 1.0 H A:ASN388 4.4 48.4 1.0 O A:HOH1005 4.4 40.3 1.0 H A:HIS387 4.5 46.5 1.0 N A:GLY529 4.5 38.2 1.0 O A:HOH841 4.5 36.2 1.0 H A:GLY529 4.5 46.0 1.0 HB2 A:PRO321 4.6 42.7 1.0 C A:HIS387 4.6 41.9 1.0 CA A:HIS387 4.6 38.6 1.0 HG2 A:PRO321 4.7 43.6 1.0 CD A:PRO321 4.8 36.6 1.0 CA A:ASN388 4.8 42.2 1.0 ND2 A:ASN388 4.9 50.1 1.0 C A:GLY529 5.0 34.9 1.0 N A:HIS387 5.0 38.6 1.0

Barium binding site 6 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 6 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 6 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba623 b:71.3 occ:0.31 O A:HOH1004 2.6 46.0 1.0 HB2 A:ASP442 3.2 38.0 1.0 O A:HOH901 3.3 32.8 1.0 HE2 A:LYS441 3.5 73.5 1.0 HA A:ASP442 3.5 38.6 1.0 HZ3 A:LYS441 4.0 74.6 1.0 CB A:ASP442 4.0 31.6 1.0 CA A:ASP442 4.1 32.0 1.0 HZ1 A:LYS441 4.2 74.6 1.0 HG2 A:LYS441 4.2 54.6 1.0 HB2 A:LYS273 4.3 46.0 1.0 HB3 A:LYS441 4.3 49.2 1.0 CE A:LYS441 4.3 61.2 1.0 NZ A:LYS441 4.3 62.1 1.0 N A:ASP442 4.4 32.9 1.0 HD2 A:LYS273 4.4 51.6 1.0 CG A:ASP442 4.5 31.9 1.0 C A:LYS441 4.7 34.7 1.0 OD1 A:ASP442 4.7 29.5 1.0 O A:LYS441 4.7 32.0 1.0 H A:ASP442 4.7 39.6 1.0 HB3 A:ASP442 4.8 38.0 1.0 HD3 A:LYS273 4.8 51.6 1.0 HD3 A:PRO443 4.9 35.8 1.0 HE3 A:LYS441 4.9 73.5 1.0 O A:HOH808 4.9 36.1 1.0 CG A:LYS441 4.9 45.5 1.0 O A:HOH910 5.0 38.3 1.0 HB3 A:LYS273 5.0 46.0 1.0

Barium binding site 7 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 7 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 7 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ M:Ba612 b:32.8 occ:0.31 H M:VAL560 2.6 32.2 1.0 HA M:HIS559 2.6 34.6 1.0 CE1 M:HIS516 2.9 35.4 1.0 HG22 M:VAL560 2.9 33.8 1.0 HE1 M:HIS516 2.9 42.6 1.0 N1 M:FAD606 3.2 25.6 1.0 NE2 M:HIS516 3.2 33.7 1.0 HB3 M:HIS559 3.2 34.4 1.0 ND1 M:HIS516 3.2 36.7 1.0 N M:VAL560 3.3 26.8 1.0 C10 M:FAD606 3.4 26.4 1.0 CA M:HIS559 3.4 28.7 1.0 H1'2 M:FAD606 3.4 30.4 1.0 HG13 M:VAL560 3.5 38.2 1.0 C2 M:FAD606 3.5 26.7 1.0 HD1 M:HIS516 3.6 44.2 1.0 ND1 M:HIS559 3.6 28.5 1.0 CB M:HIS559 3.7 28.6 1.0 CD2 M:HIS516 3.7 34.0 1.0 CG M:HIS516 3.7 32.6 1.0 CG2 M:VAL560 3.8 28.1 1.0 N10 M:FAD606 3.9 25.9 1.0 C4X M:FAD606 3.9 25.7 1.0 C M:HIS559 3.9 27.7 1.0 N3 M:FAD606 3.9 26.2 1.0 O2 M:FAD606 4.0 26.9 1.0 CG M:HIS559 4.0 28.9 1.0 C1' M:FAD606 4.1 25.2 1.0 C4 M:FAD606 4.2 26.5 1.0 HG21 M:VAL560 4.3 33.8 1.0 H1'1 M:FAD606 4.3 30.4 1.0 CG1 M:VAL560 4.3 31.8 1.0 HD2 M:HIS516 4.3 40.9 1.0 O M:HOH926 4.3 34.7 1.0 HG23 M:VAL560 4.4 33.8 1.0 CB M:VAL560 4.4 30.0 1.0 CA M:VAL560 4.4 28.6 1.0 HN3 M:FAD606 4.4 31.6 1.0 O M:HOH941 4.6 29.9 1.0 HB2 M:HIS559 4.6 34.4 1.0 O M:SER558 4.6 29.7 1.0 N5 M:FAD606 4.6 28.0 1.0 HB3 M:HIS516 4.6 37.2 1.0 N M:HIS559 4.6 28.3 1.0 C9A M:FAD606 4.7 26.6 1.0 H M:MET561 4.7 33.6 1.0 CE1 M:HIS559 4.7 29.4 1.0 HG11 M:VAL560 4.8 38.2 1.0 O M:HOH935 4.8 33.0 1.0 CB M:HIS516 4.8 30.9 1.0 HG12 M:VAL560 5.0 38.2 1.0 C5X M:FAD606 5.0 26.7 1.0

Barium binding site 8 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 8 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 8 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ M:Ba613 b:39.7 occ:0.41 H M:GLU221 2.4 44.0 1.0 HD2 M:HIS172 2.9 45.9 1.0 HD3 M:ARG147 3.1 45.2 1.0 HB3 M:HIS220 3.2 42.6 1.0 HB2 M:GLU221 3.2 50.4 1.0 N M:GLU221 3.2 36.6 1.0 HA M:HIS220 3.5 40.9 1.0 O M:HOH912 3.6 36.9 1.0 HB3 M:GLU221 3.6 50.4 1.0 HH11 M:ARG147 3.6 40.9 1.0 CD2 M:HIS172 3.7 38.1 1.0 O M:HOH931 3.7 46.9 1.0 CB M:GLU221 3.8 41.9 1.0 CB M:HIS220 3.9 35.4 1.0 NH1 M:ARG147 4.0 34.0 1.0 CA M:HIS220 4.0 34.0 1.0 CD M:ARG147 4.0 37.6 1.0 O M:HOH860 4.0 32.2 1.0 CA M:GLU221 4.1 36.8 1.0 C M:HIS220 4.1 33.6 1.0 HD2 M:ARG147 4.3 45.2 1.0 HB3 M:HIS172 4.3 41.8 1.0 HH12 M:ARG147 4.3 40.9 1.0 ND1 M:HIS220 4.4 40.3 1.0 CZ M:ARG147 4.4 35.5 1.0 CG M:HIS220 4.5 37.6 1.0 NE M:ARG147 4.5 37.3 1.0 NE2 M:HIS172 4.5 38.3 1.0 H M:ASP222 4.6 42.9 1.0 CG M:HIS172 4.6 37.5 1.0 HA M:GLU221 4.6 44.2 1.0 HB2 M:HIS220 4.7 42.6 1.0 OE1 M:GLU221 4.9 63.1 1.0 CB M:HIS172 5.0 34.8 1.0

Barium binding site 9 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 9 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 9 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ M:Ba614 b:38.3 occ:0.34 O M:HOH898 3.0 36.9 1.0 O M:HOH930 3.0 36.0 1.0 HD3 M:PRO149 3.1 44.1 1.0 HB2 M:PHE160 3.2 43.6 1.0 ND1 M:HIS158 3.2 33.8 1.0 HD1 M:PHE160 3.2 45.7 1.0 HG3 M:PRO175 3.3 40.6 1.0 HG3 M:PRO216 3.4 38.1 1.0 HG3 M:PRO149 3.4 45.9 1.0 O M:HOH949 3.4 30.9 1.0 HB3 M:HIS158 3.4 41.6 1.0 HB3 M:PRO149 3.6 43.9 1.0 CD M:PRO149 3.9 36.7 1.0 CG M:PRO149 4.0 38.2 1.0 CE1 M:HIS158 4.0 31.6 1.0 CG M:HIS158 4.0 33.7 1.0 CD1 M:PHE160 4.0 38.0 1.0 HD3 M:PRO216 4.0 36.8 1.0 HE1 M:HIS158 4.1 38.0 1.0 CB M:PHE160 4.1 36.3 1.0 CB M:HIS158 4.2 34.6 1.0 CG M:PRO216 4.2 31.7 1.0 CG M:PRO175 4.2 33.7 1.0 CB M:PRO149 4.2 36.5 1.0 N M:PRO216 4.3 30.7 1.0 HA M:PRO216 4.3 34.9 1.0 CD M:PRO216 4.4 30.6 1.0 HA M:PHE215 4.5 34.7 1.0 HB3 M:PRO216 4.5 37.4 1.0 HD3 M:PRO175 4.5 39.0 1.0 C M:PHE215 4.5 28.8 1.0 CG M:PHE160 4.5 36.7 1.0 O M:TYR159 4.5 36.1 1.0 HA M:PHE160 4.5 43.7 1.0 HD2 M:PRO149 4.6 44.1 1.0 H M:TYR159 4.6 41.8 1.0 HG2 M:PRO175 4.7 40.6 1.0 CA M:PRO216 4.7 29.0 1.0 HB3 M:PHE160 4.7 43.6 1.0 N M:PRO149 4.7 37.2 1.0 CB M:PRO216 4.7 31.1 1.0 C M:TYR159 4.8 36.2 1.0 CA M:PHE160 4.8 36.3 1.0 HB3 M:PRO175 4.8 40.5 1.0 HB2 M:HIS158 4.9 41.6 1.0 O M:PHE215 4.9 29.3 1.0 HG2 M:PRO149 4.9 45.9 1.0 CD M:PRO175 4.9 32.4 1.0 HA M:HIS158 4.9 41.0 1.0 N M:TYR159 4.9 34.7 1.0 HG2 M:PRO216 4.9 38.1 1.0 HB2 M:PRO149 5.0 43.9 1.0 N M:PHE160 5.0 36.0 1.0 HA M:PRO175 5.0 35.7 1.0 CA M:PHE215 5.0 28.8 1.0

Barium binding site 10 out of 12 in 9h7z

Barium Binding Sites List in 9h7z

Barium binding site 10 out of 12 in the Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 10 of Aspergillus Niger Glucose Oxidase Bound to BA2+ Ions within 5.0Å range: probe atom residue distance (Å) B Occ M:Ba615 b:50.1 occ:0.31 O M:HOH828 2.7 45.6 1.0 HE3 M:LYS273 3.0 65.8 1.0 HB2 M:ASP442 3.1 39.3 1.0 O M:HOH757 3.2 35.2 1.0 HG3 M:LYS441 3.3 52.7 1.0 HZ2 M:LYS441 3.3 77.7 1.0 HA M:ASP442 3.4 37.8 1.0 HD2 M:LYS273 3.4 56.3 1.0 HZ2 M:LYS273 3.4 74.4 1.0 CE M:LYS273 3.7 54.7 1.0 HZ3 M:LYS441 3.7 77.7 1.0 HG3 M:LYS273 3.8 53.1 1.0 CB M:ASP442 3.9 32.7 1.0 CD M:LYS273 3.9 46.8 1.0 NZ M:LYS441 3.9 64.7 1.0 NZ M:LYS273 4.0 61.9 1.0 CA M:ASP442 4.0 31.4 1.0 HZ1 M:LYS273 4.2 74.4 1.0 CG M:LYS441 4.2 43.8 1.0 N M:ASP442 4.3 32.5 1.0 CG M:LYS273 4.4 44.2 1.0 CG M:ASP442 4.4 32.1 1.0 HZ1 M:LYS441 4.4 77.7 1.0 OD1 M:ASP442 4.5 31.7 1.0 O M:LYS441 4.5 32.0 1.0 C M:LYS441 4.5 33.4 1.0 HE2 M:LYS273 4.6 65.8 1.0 H M:ASP442 4.6 39.1 1.0 HG2 M:LYS441 4.6 52.7 1.0 HD3 M:LYS441 4.6 61.3 1.0 HD3 M:PRO443 4.6 37.8 1.0 HB3 M:ASP442 4.7 39.3 1.0 O M:HOH781 4.7 40.7 1.0 HZ3 M:LYS273 4.7 74.4 1.0 HB2 M:LYS273 4.8 45.9 1.0 HB2 M:LYS441 4.8 47.9 1.0 HD3 M:LYS273 4.8 56.3 1.0 CD M:LYS441 4.9 51.0 1.0 O M:HOH975 4.9 41.9 1.0 HD2 M:PRO443 4.9 37.8 1.0

Reference: