Structure of PDB 3nak Chain B

Receptor sequence
>3nakB (length=595) Species: 9925 (Capra hircus) [Search protein sequence]
SWEVGCGAPVPLVTCDEQSPYRTITGDCNNRRSPALGAANRALARWLPAE
YEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLF
MQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCVQGDECFPIMFPKNDPK
LKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLA
SRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQ
AGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKIL
GAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFG
HMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL
AKNSKLMNQNKMVTSELRNKLFQPTHKVHGFDLAAINLQRCRDHGMPGYN
SWRGFCGLSQPKTLKGLQAVLKNKVLAKKLLDLYKTPDNIDIWIGGNAEP
MVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFS
RLICDNTHITKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN
3D structure
PDB3nak Crystal structure of the complex of goat lactoperoxidase with hypothiocyanite at 3.3 A resolution
ChainB
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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
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 CA B D110 T184 F186 D188 S190 D110 T184 F186 D188 S190
BS02 HEM B M101 G104 Q105 D108 D112 F113 A114 R255 E258 Q259 F347 R348 H351 R440 M101 G104 Q105 D108 D112 F113 A114 R255 E258 Q259 F347 R348 H351 R440
BS03 OSM B H109 R255 E258 H109 R255 E258
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3nak, PDBe:3nak, PDBj:3nak
PDBsum3nak
PubMed
UniProtA0A452E9Y6|PERL_CAPHI Lactoperoxidase (Gene Name=LPO)

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