BioLiP

Structure of PDB 1aet Chain A

Receptor sequence

>1aetA (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHI
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGY
VRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLEDGITFPKDAPSPFIFKTLEEQGL

3D structure

PDB

1aet A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.

Chain

Resolution

2.1 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 A174 H175 G178 K179 T180 H181 N184 S185 L232	R45 W48 P142 D143 A171 H172 G175 K176 T177 H178 N181 S182 L229
BS02	1MZ	A	H175 T180 G191 M230 D235	H172 T177 G188 M227 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

View graph for
Molecular Function

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Biological Process

PDB	RCSB:1aet, PDBe:1aet, PDBj:1aet
PDBsum	1aet
PubMed	8673607
UniProt	P00431\|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)