Structure of PDB 1ml2 Chain A

Receptor sequence
>1ml2A (length=294) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLA
WYTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFP
WISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKD
ADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTN
EFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKE
YANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB1ml2 A Novel Heme and Peroxide-Dependent Tryptophan-Tyrosine Cross-Link in a Mutant of Cytochrome c Peroxidase
ChainA
Resolution1.65 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 Y52 H175 W191 D235
Catalytic site (residue number reindexed from 1) R48 Y52 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 ZEM A P44 R48 W51 P145 D146 A147 L171 M172 A174 H175 G178 K179 T180 H181 N184 S185 W191 L232 P44 R48 W51 P145 D146 A147 L171 M172 A174 H175 G178 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1ml2, PDBe:1ml2, PDBj:1ml2
PDBsum1ml2
PubMed12684005
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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