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2C4V

H. pylori type II DHQase in complex with citrate

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 Residues13
DetailsBINDING SITE FOR RESIDUE CIT A1159
ChainResidue
AARG17
AILE106
AARG109
AARG113
AHOH2001
ATYR22
AASN76
AGLY78
AALA79
AHIS82
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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR22

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS102

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12784220
ChainResidueDetails
AASN76
AHIS82
AASP89
AARG113

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALEU103

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG17

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

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PDB entries from 2024-07-17

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