Structure of PDB 1kxm Chain A

Receptor sequence
>1kxmA (length=290) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH
ISGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWI
SSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAG
YVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGGGANNVFTNEFYL
NLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAND
QDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB1kxm Excision of a proposed electron transfer pathway in cytochrome c peroxidase and its replacement by a ligand-binding channel.
ChainA
Resolution1.74 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 D233
Catalytic site (residue number reindexed from 1) R46 H50 H173 D231
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 L230 P42 R46 W49 P143 D144 A145 L169 M170 A172 H173 G176 K177 T178 H179 N182 S183 L228
BS02 BZI A H175 K179 M228 D233 H173 K177 M226 D231 MOAD: Kd=0.14mM
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:1kxm, PDBe:1kxm, PDBj:1kxm
PDBsum1kxm
PubMed11967381
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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