Structure of PDB 3f9p Chain C

Receptor sequence
>3f9pC (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA
3D structure
PDB3f9p Essential role of proximal histidine-asparagine interaction in Mammalian peroxidases.
ChainC
Resolution2.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.2.2: myeloperoxidase.
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 BMA C F439 K505 F327 K393
BS02 HEM C E242 M243 F332 R333 G335 H336 I339 F407 L417 R424 E130 M131 F220 R221 G223 H224 I227 F295 L305 R312
BS03 CA C T168 F170 D172 S174 T56 F58 D60 S62
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:3f9p, PDBe:3f9p, PDBj:3f9p
PDBsum3f9p
PubMed19608745
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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