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8B2C

Crystal structure of type I dehydroquinase from Salmonella typhi inhibited by an epoxide derivative

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003855molecular_function3-dehydroquinate dehydratase activity
AAA0008652biological_processamino acid biosynthetic process
AAA0009073biological_processaromatic amino acid family biosynthetic process
AAA0009423biological_processchorismate biosynthetic process
AAA0016829molecular_functionlyase activity
AAA0046279biological_process3,4-dihydroxybenzoate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS01028
Number of Residues31
DetailsDEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgdadvkatvdyahahnvyVVmSNHD
ChainResidueDetails
AAAASP114-ASP144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267
ChainResidueDetails
AAAHIS143

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
ChainResidueDetails
AAALYS170

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
ChainResidueDetails
AAASER21
AAASER232

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
ChainResidueDetails
AAAGLU46
AAAARG213
AAAGLN236

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352
ChainResidueDetails
AAAARG82

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 54
ChainResidueDetails

237423

PDB entries from 2025-06-11

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