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2Q42

Ensemble refinement of the protein crystal structure of glyoxalase II from Arabidopsis thaliana gene At2g31350

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 700
ChainResidue
AHIS54
AHIS56
AHIS112
AASP131
AHOH901

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 701
ChainResidue
AHOH901
AASP58
AHIS59
AASP131
AHIS169

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 703
ChainResidue
BHIS54
BHIS56
BHIS59
BHIS112
BASP131
BHOH802

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 704
ChainResidue
BASP58
BHIS59
BASP131
BHIS169
BHOH802

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACY A 800
ChainResidue
APHE134
ASER137
ACYS138
ALYS140
AASN175
AARG248
ALYS251
AHOH922
AHOH1102

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 801
ChainResidue
BSER137
BCYS138
BLYS140
BTYR171
BASN175
BARG248
BLYS251
BHOH966

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 9979
ChainResidue
ALYS202
AHOH1116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16227621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
AASP58

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
BASP58

245663

PDB entries from 2025-12-03

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