Structure of PDB 3riw Chain B

Receptor sequence
>3riwB (length=268) Species: 347515 (Leishmania major strain Friedlin) [Search protein sequence]
TSEEPPFDIRALRADIEDMISEKLELGPSLIRLAWHEAASYDCFKKDGSP
NSASMRFKPECLYAGNKGLDIPRKALETLKKKYPQISYADLWVLAAYVAI
EYMGGPTIPFCWGRVDAKDGSVCGPDGRLPDGSKTQSHVREVFRRLGFND
QETVALIGAHTCGETHIEFSGYHGPWTHDKNGFDNSFFTQLLDEDWVLNP
KVEQMQLMDRATTKLMMLPSDVCLLLDPSYRKYVELYAKDNDRFNKDFAN
AFKKLTELGTRNLHKAPA
3D structure
PDB3riw Crystal Structure of Leishmania major Peroxidase and Characterization of the Compound I Tryptophan Radical.
ChainB
Resolution2.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R64 H68 A96 H192 W208 D253
Catalytic site (residue number reindexed from 1) R32 H36 A64 H160 W176 D221
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 B P60 R64 W67 P162 G164 L188 A191 H192 E196 T197 H198 F201 S202 W208 S252 F280 F284 P28 R32 W35 P130 G132 L156 A159 H160 E164 T165 H166 F169 S170 W176 S220 F248 F252
BS02 CA B E69 S72 S81 S86 E92 E37 S40 S49 S54 E60
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:3riw, PDBe:3riw, PDBj:3riw
PDBsum3riw
PubMed21566139
UniProtQ4Q3K2

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