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6RZ0

Crystal structure of Escherichia coli Glyoxalase II

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 Residues10
Detailsbinding site for residue GOL A 301
ChainResidue
ALEU195
AHOH573
AILE201
ATHR202
ALEU203
APRO204
AHOH443
AHOH500
AHOH552
AHOH565

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS56
AHIS181
ACL306
AHOH713

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS53
AHIS55
AHIS110
AASP127
AZN304
AHOH430

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN A 304
ChainResidue
AASP57
AHIS58
AASP127
AHIS165
AZN303
AHOH430

site_idAC5
Number of Residues6
Detailsbinding site for residue CXS A 305
ChainResidue
AASN186
AASP187
AARG190
AASP249
AHOH621
AHOH832

site_idAC6
Number of Residues5
Detailsbinding site for residue CL A 306
ChainResidue
AHIS56
ALEU179
APRO180
AHIS181
AZN302

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 307
ChainResidue
AHIS110
AARG136

site_idAC8
Number of Residues1
Detailsbinding site for residue ZN A 308
ChainResidue
AHIS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q16775","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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