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1J2Y

Crystal structure of the type II 3-dehydroquinase

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
A0019631biological_processquinate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DQA A 219
ChainResidue
AARG17
AILE106
AARG113
ATYR22
AASN76
AGLY78
AHIS82
AASP89
AHIS102
ALEU103
ATHR104

Functional Information from PROSITE/UniProt
site_idPS01029
Number of Residues18
DetailsDEHYDROQUINASE_II Dehydroquinase class II signature. IQGPNLnmLGhRDprlYG
ChainResidueDetails
AILE6-GLY23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12784220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1uqr
ChainResidueDetails
AARG109
AHIS102
ATYR22
AASN10
AGLU100
AARG17

243083

PDB entries from 2025-10-15

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