Structure of PDB 2v2e Chain A

Receptor sequence
>2v2eA (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNAIGYGPVLVRLAWHT
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADY
VRTFFQRLNMNDREVVALMGAHALGKTHLKRSGYEGPWGAANNVFTNEFY
LNLLNENWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2v2e The Tuberculosis Prodrug Isoniazid Bound to Activating Peroxidases.
ChainA
Resolution1.68 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R48 H52 H175 W191 D235
Catalytic site (residue number reindexed from 1) R45 H49 H172 W188 D232
Enzyme Commision number 1.11.1.5: cytochrome-c peroxidase.
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 HEM A P44 R48 W51 P145 D146 A147 L171 M172 A174 H175 L177 G178 K179 T180 H181 R184 S185 W191 L232 P41 R45 W48 P142 D143 A144 L168 M169 A171 H172 L174 G175 K176 T177 H178 R181 S182 W188 L229
BS02 ISZ A H52 P145 H49 P142
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress

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Molecular Function
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Biological Process
External links
PDB RCSB:2v2e, PDBe:2v2e, PDBj:2v2e
PDBsum2v2e
PubMed18056997
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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