BioLiP

Structure of PDB 1dj1 Chain A

Receptor sequence

>1dj1A (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVALAWHI
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGY
VRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL

3D structure

PDB

1dj1 Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase.

Chain

Resolution

1.93 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	A48 H52 H175 W191 D235
Catalytic site (residue number reindexed from 1)	A45 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	A48 W51 P145 D146 M172 A174 H175 L177 K179 T180 H181 N184 S185 W191 L232	A45 W48 P142 D143 M169 A171 H172 L174 K176 T177 H178 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

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:1dj1, PDBe:1dj1, PDBj:1dj1
PDBsum	1dj1
PubMed	10722697
UniProt	P00431\|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)