Structure of PDB 3e2n Chain A

Receptor sequence
>3e2nA (length=282) Species: 3888,559292 [Search protein sequence]
HVASVEKGRSYEDFQKVYNAIALKIAEKKCGPVLVRLAWHTSGTWDKHDN
TGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGG
VTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLN
MNDREVVALMGAHALGKTHLKRSGYEGPFGAANNVFTNEFYLNLLNEDWK
LEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYANDQDKFFKDF
SKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
3D structure
PDB3e2n Engineering ascorbate peroxidase activity into cytochrome c peroxidase.
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R41 H45 H168 F184 D228
Catalytic site (residue number reindexed from 1) R36 H40 H163 F179 D223
Enzyme Commision number 1.11.1.11: L-ascorbate peroxidase.
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 P37 R41 W44 P138 D139 A140 L164 M165 A167 H168 G171 K172 T173 H174 R177 S178 L225 P32 R36 W39 P133 D134 A135 L159 M160 A162 H163 G166 K167 T168 H169 R172 S173 L220
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:3e2n, PDBe:3e2n, PDBj:3e2n
PDBsum3e2n
PubMed18771292
UniProtP00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial (Gene Name=CCP1);
P48534|APX1_PEA L-ascorbate peroxidase, cytosolic (Gene Name=APX1)

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