Structure of PDB 4oek Chain A

Receptor sequence
>4oekA (length=595) Species: 9925 (Capra hircus) [Search protein sequence]
SWEVGCGAPVPLVTCDEQSPYRTITGDCNNRRSPALGAANRALARWLPAE
YEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLF
MQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCVQGDECFPIMFPKNDPK
LKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLA
SRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQ
AGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKIL
GAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFG
HMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL
AKNSKLMNQNKMVTSELRNKLFQPTHKVHGFDLAAINLQRCRDHGMPGYN
SWRGFCGLSQPKTLKGLQAVLKNKVLAKKLLDLYKTPDNIDIWIGGNAEP
MVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFS
RLICDNTHITKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN
3D structure
PDB4oek Crystal Structure of the Complex of goat Lactoperoxidase with Phenylethylamine at 2.47 A
ChainA
Resolution2.47 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q105 D108 H109 D110 T184 F186 D188 S190 R255 E258 H351
Catalytic site (residue number reindexed from 1) Q105 D108 H109 D110 T184 F186 D188 S190 R255 E258 H351
Enzyme Commision number 1.11.1.7: peroxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress

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Molecular Function

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Biological Process
External links
PDB RCSB:4oek, PDBe:4oek, PDBj:4oek
PDBsum4oek
PubMed
UniProtA0A452E9Y6|PERL_CAPHI Lactoperoxidase (Gene Name=LPO)

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