Structure of PDB 2eun Chain A

Receptor sequence
>2eunA (length=292) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH
ISGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWI
SSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAG
YVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAANNVFTNEF
YLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYA
NDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2eun Probing molecular docking in a charged model binding site.
ChainA
Resolution1.7 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 G191 D235
Catalytic site (residue number reindexed from 1) R46 H50 H173 G189 D233
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 L177 G178 K179 T180 H181 N184 S185 L232 F266 R46 W49 P143 D144 A145 L169 M170 A172 H173 L175 G176 K177 T178 H179 N182 S183 L230 F264
BS02 LG3 A H175 G178 K179 T180 G191 M230 M231 L232 D235 H173 G176 K177 T178 G189 M228 M229 L230 D233 MOAD: Kd=0.05mM
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:2eun, PDBe:2eun, PDBj:2eun
PDBsum2eun
PubMed16490206
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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