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5WRF

Crystal structure of dodecameric type II dehydroquinate dehydratase from Acinetobacter baumannii with unexplained connecting electron density between free cysteine residues of molecular pairs

Functional Information from GO Data
ChainGOidnamespacecontents
A0003855molecular_function3-dehydroquinate dehydratase activity
A0009423biological_processchorismate biosynthetic process
A0019631biological_processquinate catabolic process
B0003855molecular_function3-dehydroquinate dehydratase activity
B0009423biological_processchorismate biosynthetic process
B0019631biological_processquinate catabolic process
C0003855molecular_function3-dehydroquinate dehydratase activity
C0009423biological_processchorismate biosynthetic process
C0019631biological_processquinate catabolic process
D0003855molecular_function3-dehydroquinate dehydratase activity
D0009423biological_processchorismate biosynthetic process
D0019631biological_processquinate catabolic process
E0003855molecular_function3-dehydroquinate dehydratase activity
E0009423biological_processchorismate biosynthetic process
E0019631biological_processquinate catabolic process
F0003855molecular_function3-dehydroquinate dehydratase activity
F0009423biological_processchorismate biosynthetic process
F0019631biological_processquinate catabolic process
G0003855molecular_function3-dehydroquinate dehydratase activity
G0009423biological_processchorismate biosynthetic process
G0019631biological_processquinate catabolic process
H0003855molecular_function3-dehydroquinate dehydratase activity
H0009423biological_processchorismate biosynthetic process
H0019631biological_processquinate catabolic process
I0003855molecular_function3-dehydroquinate dehydratase activity
I0009423biological_processchorismate biosynthetic process
I0019631biological_processquinate catabolic process
J0003855molecular_function3-dehydroquinate dehydratase activity
J0009423biological_processchorismate biosynthetic process
J0019631biological_processquinate catabolic process
K0003855molecular_function3-dehydroquinate dehydratase activity
K0009423biological_processchorismate biosynthetic process
K0019631biological_processquinate catabolic process
L0003855molecular_function3-dehydroquinate dehydratase activity
L0009423biological_processchorismate biosynthetic process
L0019631biological_processquinate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 201
ChainResidue
AALA78
AHIS82
AVAL106
AARG113

Functional Information from PROSITE/UniProt
site_idPS01029
Number of Residues18
DetailsDEHYDROQUINASE_II Dehydroquinase class II signature. IHGPNLnlLGkREpevYG
ChainResidueDetails
AILE8-GLY25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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