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2ZJF

Crystal structure of Mycobacterium tuberculosis epoxide hydrolase B complexed with an inhibitor

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 Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 357
ChainResidue
APRO37
ATHR190
ATYR256
ATRP334
AGLN337

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 358
ChainResidue
AARG63
AGLU81
ATHR176

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 359
ChainResidue
AASP166
AALA169
ATYR272
AASP276
AHOH367
AHIS153

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BSU A 360
ChainResidue
APHE36
AASP104
ATRP105
AILE137
ATYR164
ALEU189
ATYR272
AHIS333
ATRP334

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

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PDB entries from 2024-09-11

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