Structure of PDB 1cxp Chain C

Receptor sequence
>1cxpC (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA
3D structure
PDB1cxp X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
ChainC
Resolution1.8 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) R127
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 FUC C V320 R504 V208 R392
BS02 MAN C F439 K505 F327 K393
BS03 HEM C E242 M243 T329 R333 G335 H336 I339 F365 F407 L417 R424 E130 M131 T217 R221 G223 H224 I227 F253 F295 L305 R312
BS04 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:1cxp, PDBe:1cxp, PDBj:1cxp
PDBsum1cxp
PubMed10766826
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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