Structure of PDB 2eut Chain A

Receptor sequence
>2eutA (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHI
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGY
VRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB2eut Probing molecular docking in a charged model binding site.
ChainA
Resolution1.12 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) R45 H49 H172 G188 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 N184 S185 L232 R45 W48 P142 D143 A144 L168 M169 A171 H172 G175 K176 T177 H178 N181 S182 L229
BS02 BVF A H175 K179 T180 G191 M230 M231 D235 H172 K176 T177 G188 M227 M228 D232
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:2eut, PDBe:2eut, PDBj:2eut
PDBsum2eut
PubMed16490206
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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