Structure of PDB 2b12 Chain A

Receptor sequence
>2b12A (length=294) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLA
WHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFP
WISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKD
ADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTN
EFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKE
YANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2b12 Effects of interface mutations on association modes and electron-transfer rates between proteins
ChainA
Resolution3.02 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) R48 H52 H175 W191 D235
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 ZNH A P44 V45 R48 W51 P145 F158 M172 A174 H175 G178 K179 T180 H181 S185 P44 V45 R48 W51 P145 F158 M172 A174 H175 G178 K179 T180 H181 S185
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:2b12, PDBe:2b12, PDBj:2b12
PDBsum2b12
PubMed16227441
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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