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1QH5

HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004416molecular_functionhydroxyacylglutathione hydrolase activity
A0019243biological_processobsolete methylglyoxal catabolic process to pyruvate via (R)-S-lactoyl-glutathione
B0004416molecular_functionhydroxyacylglutathione hydrolase activity
B0019243biological_processobsolete methylglyoxal catabolic process to pyruvate via (R)-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
AHOH464
AHOH465

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AASP58
AHIS59
AASP134
AHIS173
AZN261
AGSH463
AHOH464

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 261
ChainResidue
BHIS54
BHIS56
BHIS110
BASP134
BZN262
BGBP464
BHOH466

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 262
ChainResidue
BASP58
BHIS59
BASP134
BHIS173
BZN261
BGBP464
BHOH466

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH A 463
ChainResidue
AASP58
AHIS110
AASP134
APHE137
ACYS141
AGLY142
ALYS143
ATYR145
AHIS173
ATYR175
AARG249
ALYS252
AZN262
AHOH464
AHOH465
AHOH477
AHOH553

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GBP B 464
ChainResidue
BHIS56
BASP58
BHIS110
BASP134
BPHE137
BCYS141
BGLY142
BLYS143
BTYR145
BHIS173
BTYR175
BARG249
BLYS252
BZN261
BZN262
BHOH466
BHOH478
BHOH555

site_idZNA
Number of Residues10
DetailsBINUCLEAR ZINC BINDING SITE IN A MOLECULE
ChainResidue
AHIS54
AHIS173
AHIS56
AHIS110
AASP134
AGSH463
AHOH464
AHOH465
AASP58
AHIS59

site_idZNB
Number of Residues9
DetailsBINUCLEAR ZINC BINDING SITE IN B MOLECULE
ChainResidue
BHIS54
BHIS56
BHIS110
BASP134
BGBP464
BHOH466
BASP58
BHIS59
BHIS173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10508780","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KB8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99KB8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10508780, 11085979
ChainResidueDetails
AASP58

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10508780, 11085979
ChainResidueDetails
BASP58

site_idMCSA1
Number of Residues7
DetailsM-CSA 157
ChainResidueDetails
AHIS54metal ligand
AHIS56metal ligand
AASP58activator, electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
AHIS59metal ligand
AHIS110metal ligand
AASP134metal ligand
AHIS173metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 157
ChainResidueDetails
BHIS54metal ligand
BHIS56metal ligand
BASP58activator, electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
BHIS59metal ligand
BHIS110metal ligand
BASP134metal ligand
BHIS173metal ligand

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PDB entries from 2026-02-25

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