Structure of PDB 5d6m Chain A

Receptor sequence
>5d6mA (length=291) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYENYIGYGPELVRLAWHI
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGY
VRTFFQRLNMNDREVVALMGAHALGKTELKNSGYEGPWGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB5d6m Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions.
ChainA
Resolution1.653 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 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 P44 R48 W51 P145 D146 A147 L171 M172 A174 H175 G178 K179 T180 E181 N184 S185 W191 L232 P41 R45 W48 P142 D143 A144 L168 M169 A171 H172 G175 K176 T177 E178 N181 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

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Molecular Function
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Biological Process
External links
PDB RCSB:5d6m, PDBe:5d6m, PDBj:5d6m
PDBsum5d6m
PubMed26885726
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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