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4CKY

Structure of the Mycobacterium tuberculosis Type II Dehydroquinase inhibited by a 3-dehydroquinic acid derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0003855molecular_function3-dehydroquinate dehydratase activity
A0005829cellular_componentcytosol
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 Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1144
ChainResidue
AASN6
AGLU70
AHOH2052
AHOH2143

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1145
ChainResidue
ALEU128
AILE130
AGLN131
AHIS143

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1146
ChainResidue
AARG113
AHIS114
AHOH2090
AHOH2128
AARG87

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1147
ChainResidue
ASER54
ASER54
ASER54
AHOH2065
AHOH2065
AHOH2065
AHOH2144
AHOH2144
AHOH2144

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ND3 A 1148
ChainResidue
AASN75
AGLY77
AGLY78
AHIS81
AASP88
AHIS101
AILE102
ASER103
AARG108
AARG112
AHOH2007

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR24

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS101

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AARG112
AASN75
AHIS81
AASP88
AILE102

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG19

221051

PDB entries from 2024-06-12

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