Structure of PDB 1myp Chain C

Receptor sequence
>1mypC (length=462) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
NCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQ
INALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPF
DNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATE
LKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTY
RSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSR
VFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRI
GLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARK
LMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFW
WENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVN
CSTLPALNLASW
3D structure
PDB1myp X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
ChainC
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R239
Catalytic site (residue number reindexed from 1) R126
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 CA C T168 F170 D172 S174 T55 F57 D59 S61
BS02 HEM C E242 M243 T329 R333 H336 I339 F365 L406 F407 R424 E129 M130 T216 R220 H223 I226 F252 L293 F294 R311
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:1myp, PDBe:1myp, PDBj:1myp
PDBsum1myp
PubMed1320128
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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