Structure of PDB 3gck Chain A

Receptor sequence

>3gckA (length=595) Species: 9913 (Bos taurus)

SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAE
YEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLF
MQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPK
LKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLA
SRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFL
AGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKIL
GAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFG
HMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL
AKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYN
SWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEP
MVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFS
RLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN

3D structure

• PDB: 3gck Mode of ligand binding and assignment of subsites in mammalian peroxidases: crystal structure of lactoperoxidase complexes with acetyl salycylic acid, salicylhydroxamic acid and benzylhydroxamic acid
• Chain: A
• Resolution: 2.9 Å

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	HEM	A	M101 G104 Q105 D108 D112 F113 E258 Q259 F347 R348 G350 H351 V354 I436 R440	M101 G104 Q105 D108 D112 F113 E258 Q259 F347 R348 G350 H351 V354 I436 R440
BS02	CA	A	D110 T184 F186 D188 S190	D110 T184 F186 D188 S190
BS03	BHO	A	H109 R255 E258 F381 P424	H109 R255 E258 F381 P424

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0020037 heme binding

Biological Process

• GO:0006979 response to oxidative stress

External links

• PDB: RCSB:3gck, PDBe:3gck, PDBj:3gck
• PDBsum: 3gck
• UniProt: P80025|PERL_BOVIN Lactoperoxidase (Gene Name=LPO)