Structure of PDB 2n18 Chain A

Receptor sequence
>2n18A (length=294) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLA
WHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFP
WISSGDLFSLGGVTAVQEMQGPKIPWRAGRVDTPEDTTPDNGRLPDADKD
ADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNCFTN
EFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKE
YANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2n18 The low-affinity complex of cytochrome c and its peroxidase.
ChainA
ResolutionN/A
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) 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 HEM A P44 R48 W51 P145 A147 L171 M172 A174 H175 K179 T180 H181 N184 S185 W191 L232 P44 R48 W51 P145 A147 L171 M172 A174 H175 K179 T180 H181 N184 S185 W191 L232
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:2n18, PDBe:2n18, PDBj:2n18
PDBsum2n18
PubMed25944250
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

[Back to BioLiP]