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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
BCYS104
BALA106
BTHR107
BGLU158
BPHE182
BALA191
BTYR221
ACYS104
AALA106
ATHR107
AGLU158
APHE182
AALA191
ATYR221
BVAL102

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

218853

PDB entries from 2024-04-24

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