Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4B6P

Structure of Mycobacterium tuberculosis Type II Dehydroquinase inhibited by (2S)-2-Perfluorobenzyl-3-dehydroquinic 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 Residues16
DetailsBINDING SITE FOR RESIDUE 2HN A 1145
ChainResidue
AASN12
AHIS81
AASP88
AHIS101
AILE102
ASER103
AARG112
AHOH2003
ALEU13
AARG15
ALEU16
AARG19
ATYR24
AASN75
AGLY77
AGLY78

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1146
ChainResidue
ASER54
ASER54
ASER54
AALA56
AALA56
AALA56
AHOH2024
AHOH2024
AHOH2024

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1147
ChainResidue
AARG50
ATRP61
AGLN64
AHOH2027

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
AASN75
AHIS81
AASP88
AILE102
AARG112

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG19

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon