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2OCZ

The Structure of a Putative 3-Dehydroquinate Dehydratase from Streptococcus pyogenes.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003855molecular_function3-dehydroquinate dehydratase activity
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016829molecular_functionlyase activity
A0046279biological_process3,4-dihydroxybenzoate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASN89
AHOH505
AHOH533
AHOH552
AHOH707
AHOH711

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
AHOH627
AHOH665
AHOH790
AGLN105
ALEU108
ALEU137

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ALEU108
APHE110
AHOH536
AHOH639
AHOH774

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLY179
AARG186
AGLY208
AGLN209

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ATYR117
APRO124
AASN126
AHOH599
AHOH631
AHOH772

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
AHIS118

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
ALYS143

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
AGLU30
AARG62
AARG186
ASER205
AGLN209

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
AHIS118
ALYS143
AGLU66

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PDB entries from 2024-11-06

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