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6S0I

Crystal structure of Escherichia coli Glyoxalase II with L-Tartrate in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004416molecular_functionhydroxyacylglutathione hydrolase activity
A0008270molecular_functionzinc ion binding
A0009408biological_processresponse to heat
A0009636biological_processresponse to toxic substance
A0016787molecular_functionhydrolase activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue ZN A 401
ChainResidue
AASP57
AHIS58
AASP127
AHIS165
AZN402
ATLA403
AHOH564

site_idAC2
Number of Residues8
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS58
AHIS110
AASP127
AZN401
ATLA403
AHOH564
AHIS53
AHIS55

site_idAC3
Number of Residues15
Detailsbinding site for residue TLA A 403
ChainResidue
AASN12
AHIS55
AASP57
AHIS58
AHIS110
AASP127
APHE138
AHIS165
AZN401
AZN402
AHOH514
AHOH564
AHOH574
AHOH634
AHOH655

site_idAC4
Number of Residues6
Detailsbinding site for residue EPE A 404
ChainResidue
ACYS134
ASER170
AARG245
ALYS248
AHOH536
AHOH679

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q16775
ChainResidueDetails
AHIS53
AHIS55
AASP57
AHIS58
AHIS110
AASP127
AARG136
AHIS165
AARG245

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PDB entries from 2024-07-24

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