Structure of PDB 1d5l Chain D

Receptor sequence

>1d5lD (length=466) Species: 9606 (Homo sapiens)

VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA

3D structure

• PDB: 1d5l Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
• Chain: D
• Resolution: 1.9 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	HEM	D	E242 M243 T329 R333 G335 H336 I339 F365 F407 L417 R424	E130 M131 T217 R221 G223 H224 I227 F253 F295 L305 R312
BS04	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:1d5l, PDBe:1d5l, PDBj:1d5l
• PDBsum: 1d5l
• PubMed: 11705390
• UniProt: P05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)