Structure of PDB 3m2e Chain A

Receptor sequence
>3m2eA (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHT
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADY
VRTFFQRLNMNDREVVALMGAHALGKTHLKRSGYEGPWGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB3m2e Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 R48 W51 P145 D146 A147 L171 M172 A174 H175 G178 K179 T180 H181 R184 S185 W191 L232 R45 W48 P142 D143 A144 L168 M169 A171 H172 G175 K176 T177 H178 R181 S182 W188 L229
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3m2e, PDBe:3m2e, PDBj:3m2e
PDBsum3m2e
PubMed20230048
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

[Back to BioLiP]