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1QH3

HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004416molecular_functionhydroxyacylglutathione hydrolase activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
B0004416molecular_functionhydroxyacylglutathione hydrolase activity
B0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 261
ChainResidue
AHIS54
AHIS56
AHIS110
AASP134
AZN262
ACAC463
AHOH468

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AASP58
AHIS59
AASP134
AHIS173
AZN261
ACAC463
AHOH468

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CAC A 463
ChainResidue
AHIS56
AASP58
AHIS110
AASP134
ATYR145
AHIS173
AZN261
AZN262
AHOH468
AHOH506

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 464
ChainResidue
APHE137
ACYS141
ALYS143
ATYR175
AARG249
ALYS252
AHOH471
AHOH507
AHOH521

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CAC A 265
ChainResidue
ACYS153
AGLU158

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 266
ChainResidue
AHIS185
AHIS235
AGLU251
ACL467

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 467
ChainResidue
AMN266
BMN266

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 261
ChainResidue
BHIS54
BHIS56
BHIS110
BASP134
BZN262
BCAC469
BHOH473

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 262
ChainResidue
BASP58
BHIS59
BASP134
BHIS173
BZN261
BCAC469
BHOH473

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CAC B 469
ChainResidue
BHIS56
BASP58
BHIS110
BASP134
BHIS173
BTYR175
BZN261
BZN262
BHOH473
BHOH511
BHOH616

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 468
ChainResidue
BPHE137
BCYS141
BTYR175
BARG249
BLYS252
BHOH476
BHOH512

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CAC B 265
ChainResidue
BCYS153
BLYS154
BGLU158

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 266
ChainResidue
BHOH659
ACL467
BHIS185
BGLU251
BHOH527
BHOH554

site_idZNA
Number of Residues9
DetailsBINUCLEAR ZINC BINDING SITE IN A MOLECULE
ChainResidue
AHIS54
AHIS56
AHIS110
AASP134
ACAC463
AHOH468
AASP58
AHIS59
AHIS173

site_idZNB
Number of Residues9
DetailsBINUCLEAR ZINC BINDING SITE IN B MOLECULE
ChainResidue
BHIS54
BHIS56
BHIS110
BASP134
BCAC469
BHOH473
BASP58
BHIS59
BHIS173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:10508780
ChainResidueDetails
AVAL102
AGLU158
APHE182
AALA191
ATYR221
BVAL102
BCYS104
BALA106
BTHR107
BGLU158
BPHE182
BALA191
BTYR221
ACYS104
AALA106
ATHR107

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8
ChainResidueDetails
ACYS116
BCYS116

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KB8
ChainResidueDetails
AGLU229
BGLU229

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 157
ChainResidueDetails
AVAL102metal ligand
ACYS104metal ligand
AALA106activator, electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
ATHR107metal ligand
AGLU158metal ligand
APHE182metal ligand
ATYR221metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 157
ChainResidueDetails
BVAL102metal ligand
BCYS104metal ligand
BALA106activator, electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
BTHR107metal ligand
BGLU158metal ligand
BPHE182metal ligand
BTYR221metal ligand

218500

数据于2024-04-17公开中

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