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2YR1

Crystal Structure of 3-dehydroquinate dehydratase from Geobacillus kaustophilus HTA426

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
B0003855molecular_function3-dehydroquinate dehydratase activity
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016829molecular_functionlyase activity
B0046279biological_process3,4-dihydroxybenzoate biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
AHIS147
BHIS147

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
ALYS174
BLYS174

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214
ChainResidueDetails
AGLU50
BGLN239
AARG86
AARG216
ASER235
AGLN239
BGLU50
BARG86
BARG216
BSER235

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
AGLU90
ALYS174
AHIS147

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
BGLU90
BLYS174
BHIS147

223532

PDB entries from 2024-08-07

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