Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2E3J

The crystal structure of epoxide hydrolase B (Rv1938) from mycobacterium tuberculosis at 2.1 angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004301molecular_functionepoxide hydrolase activity
A0009636biological_processresponse to toxic substance
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 2001
ChainResidue
AVAL73
ATHR176

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 2002
ChainResidue
ATYR167
AVAL170
AGLY173

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 2003
ChainResidue
ATHR190
ATYR256
ATRP334

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 2004
ChainResidue
AHIS153
AASP166
ATYR272
AHIS273
AASP276
ASER150

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 2005
ChainResidue
APHE36
ATYR164
ALEU226
ATYR272
AHIS333

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 2006
ChainResidue
AALA53

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 2007
ChainResidue
AMET228
AGLY231
AALA232
AHOH2115

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 2008
ChainResidue
AHIS45
APRO48
AALA49
AHIS117
AASP119
AASN344

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 2009
ChainResidue
AGLY94
AGLU96
AHOH2132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:18585390
ChainResidueDetails
AASP104

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:18585390
ChainResidueDetails
AHIS333

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to the formation of an oxyanion binding site for the epoxide oxygen of substrate => ECO:0000305|PubMed:18585390
ChainResidueDetails
ATYR164
ATYR272

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Plays an orienting role for the imidazole group of His-333 => ECO:0000305|PubMed:18585390
ChainResidueDetails
AASP302

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b6g
ChainResidueDetails
AASP302
AASP104
AHIS333

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon