Structure of PDB 1aeq Chain A

Receptor sequence
>1aeqA (length=291) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHI
SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWIS
SGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGY
VRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAANNVFTNEFY
LNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLEDGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB1aeq Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein.
ChainA
Resolution2.1 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 M172 A174 H175 G178 K179 T180 H181 N184 S185 L232 R45 W48 P142 D143 M169 A171 H172 G175 K176 T177 H178 N181 S182 L229
BS02 2EZ A H175 T180 F202 M230 M231 L232 D235 H172 T177 F199 M227 M228 L229 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1aeq, PDBe:1aeq, PDBj:1aeq
PDBsum1aeq
PubMed11812152
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1)

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