Structure of PDB 1dse Chain A

Receptor sequence
>1dseA (length=292) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH
ISGTWDKHDNTGGSYGGTYRFKKQFNDPSNAGLQNGFKFLEPIHKEFPWI
SSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAG
YVRTFFQRLNMNDREVVALMGAGALGKTHLKNSGYEGPWGAANNVFTNEF
YLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYA
NDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB1dse Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
ChainA
Resolution2.0 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 G175 W191 D235
Catalytic site (residue number reindexed from 1) R46 H50 G173 W189 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 PO4 A R48 W51 R46 W49
BS02 HEM A P44 R48 W51 P145 D146 A147 L171 M172 A174 K179 T180 H181 N184 S185 L232 P42 R46 W49 P143 D144 A145 L169 M170 A172 K177 T178 H179 N182 S183 L230
BS03 IMD A M172 W191 D235 M170 W189 D233
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:1dse, PDBe:1dse, PDBj:1dse
PDBsum1dse
PubMed11170452
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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