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1FA8

CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004462molecular_functionlactoylglutathione lyase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009636biological_processresponse to toxic substance
A0016151molecular_functionnickel cation binding
A0016829molecular_functionlyase activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0004462molecular_functionlactoylglutathione lyase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009636biological_processresponse to toxic substance
B0016151molecular_functionnickel cation binding
B0016829molecular_functionlyase activity
B0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00934
Number of Residues22
DetailsGLYOXALASE_I_1 Glyoxalase I signature 1. HTmLrVgdlqRSidFYtkvLGM
ChainResidueDetails
AHIS5-MET26

site_idPS00935
Number of Residues13
DetailsGLYOXALASE_I_2 Glyoxalase I signature 2. GT.....AYGHIAlSvdN
ChainResidueDetails
AGLY69-ASN81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AGLU122
BGLU122

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10913283
ChainResidueDetails
AHIS5
AGLU56
BHIS5
BGLU56

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG9
AASN60
BARG9
BASN60

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250
ChainResidueDetails
AHIS74
BHIS74

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: in other chain => ECO:0000269|PubMed:10913283
ChainResidueDetails
AGLU122
BGLU122

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fro
ChainResidueDetails
AGLU122

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fro
ChainResidueDetails
BGLU122

site_idMCSA1
Number of Residues4
DetailsM-CSA 359
ChainResidueDetails
AHIS5metal ligand
AGLU56hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AHIS74metal ligand
AGLU122hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues4
DetailsM-CSA 359
ChainResidueDetails
BHIS5metal ligand
BGLU56hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
BHIS74metal ligand
BGLU122hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay

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PDB entries from 2024-11-13

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