Structure of PDB 1cxp Chain D

Receptor sequence

>1cxpD (length=466) Species: 9606 (Homo sapiens)

VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA

3D structure

• PDB: 1cxp X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
• Chain: D
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T168 F170 D172 S174 R239 E242 H336
• Catalytic site (residue number reindexed from 1): T56 F58 D60 S62 R127 E130 H224
• 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	MAN	D	F439 K505	F327 K393
BS02	FUC	D	V320 R504	V208 R392
BS03	CL	D	N326 V327 W436	N214 V215 W324
BS04	HEM	D	R239 E242 M243 T329 F332 R333 H336 F407 L417 L420 R424	R127 E130 M131 T217 F220 R221 H224 F295 L305 L308 R312
BS05	CA	D	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

External links

• PDB: RCSB:1cxp, PDBe:1cxp, PDBj:1cxp
• PDBsum: 1cxp
• PubMed: 10766826
• UniProt: P05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)