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1H0R

Type II Dehydroquinase from Mycobacterium tuberculosis complexed with 2,3-anhydro-quinic acid

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 Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
ASER54
AHOH2152
AHOH2153

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
AARG87
AARG113
AHIS114

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AHIS106

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FA1 A 200
ChainResidue
AGLY77
AGLY78
AHIS81
AASP88
AHIS101
AILE102
ASER103
AVAL105
AARG112
ATYR24
AASN75

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
ATRP61
AGLN64
AHOH2078

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
AGLY25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AILE102

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AALA76
ATHR82
AALA89
ASER103
AARG113

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AGLU20

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1uqr
ChainResidueDetails
ATYR24
AGLU99
AHIS101
AASN12
AARG108

219140

PDB entries from 2024-05-01

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