Structure of PDB 2zjf Chain A

Receptor sequence
>2zjfA (length=346) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
VHRILNCRGTRIHAVADSPPDQQGPLVVLLHGFPESWYSWRHQIPALAGA
GYRVVAIDQRGYGRSSKYRVQKAYRIKELVGDVVGVLDSYGAEQAFVVGH
DWGAPVAWTFAWLHPDRCAGVVGISVPFAGRGVIGLPGSPFGERRPSDYH
LELAGPGRVWYQDYFAVQDGIITEIEEDLRGWLLGLTYTVSGEGMMAATK
AAVSMDPIDVIRAGPLCMAEGARLKDAFVYPETMPAWFTEADLDFYTGEF
ERSGFGGPLSFYHNIDNDWHDLADQQGKPLTPPALFIGGQYDVGTIWGAQ
AIERAHEVMPNYRGTHMIADVGHWIQQEAPEETNRLLLDFLGGLRP
3D structure
PDB2zjf The molecular structure of epoxide hydrolase B from Mycobacterium tuberculosis and its complex with a urea-based inhibitor.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F36 D104 W105 I127 Y164 Y272 D302 H333
Catalytic site (residue number reindexed from 1) F33 D101 W102 I124 Y161 Y262 D292 H323
Enzyme Commision number 3.3.2.10: soluble epoxide hydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BSU A D104 W105 I137 Y164 V193 Y272 H333 W334 D101 W102 I134 Y161 V190 Y262 H323 W324 MOAD: ic50=19nM
PDBbind-CN: -logKd/Ki=7.72,IC50=19nM
BindingDB: IC50=19nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004301 epoxide hydrolase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0009636 response to toxic substance

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2zjf, PDBe:2zjf, PDBj:2zjf
PDBsum2zjf
PubMed18585390
UniProtP95276|EPHB_MYCTO Epoxide hydrolase B (Gene Name=MT1988)

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