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1H05

3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AARG19
AASN75
AILE102
ASER103
AHOH2119
AHOH2191
AHOH2192
AHOH2193
AHOH2194

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
ASER54
AHOH2095
AHOH2195

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AARG50
ATRP61
AGLN64
AHOH2101
AHOH2197

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
AARG15
ALEU16
AGLY17
AARG19
AHOH2199
AHOH2200

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

220113

PDB entries from 2024-05-22

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