Structure of PDB 2cep Chain A

Receptor sequence
>2cepA (length=293) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAW
HISGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPW
ISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDA
GYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNE
FYLNLLNEDWKLEKNDANNEQWDSKSGYIMLPTDYSLIQDPKYLSIVKEY
ANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2cep Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II.
ChainA
Resolution2.2 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) R47 H51 H174 W190 D234
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 G178 K179 T180 H181 N184 S185 W191 P43 R47 W50 P144 D145 A146 L170 M171 A173 H174 G177 K178 T179 H180 N183 S184 W190
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:2cep, PDBe:2cep, PDBj:2cep
PDBsum2cep
PubMed8038157
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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