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1XM8

X-RAY 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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 700
ChainResidue
AHIS54
AHIS56
AHIS112
AASP131
AFE701
AHOH901

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 701
ChainResidue
AHIS169
AZN700
AHOH901
AASP58
AHIS59
AASP131

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 703
ChainResidue
BHIS54
BHIS56
BHIS112
BASP131
BFE704
BHOH802

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 704
ChainResidue
BASP58
BHIS59
BASP131
BHIS169
BZN703
BHOH802

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 800
ChainResidue
APHE134
ASER137
ACYS138
ALYS140
AARG248
ALYS251
AHOH1099

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 900
ChainResidue
ALYS202
AHOH1113

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 801
ChainResidue
BPHE134
BSER137
BCYS138
BLYS140
BARG248
BLYS251
BHOH968

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:16227621, ECO:0000269|PubMed:17850744
ChainResidueDetails
AHIS54
BASP58
BHIS59
BHIS112
BASP131
BHIS169
AHIS56
AASP58
AHIS59
AHIS112
AASP131
AHIS169
BHIS54
BHIS56

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

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PDB entries from 2024-07-17

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