Structure of PDB 1d7w Chain D

Receptor sequence
>1d7wD (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA
3D structure
PDB1d7w Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 BR D N326 V327 W436 N214 V215 W324
BS03 HEM D E242 M243 T329 F332 R333 G335 H336 F407 L417 L420 R424 E130 M131 T217 F220 R221 G223 H224 F295 L305 L308 R312
BS04 CA D T168 F170 D172 S174 T56 F58 D60 S62
BS05 BR D I543 T545 I431 T433
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
View graph for
Biological Process
External links
PDB RCSB:1d7w, PDBe:1d7w, PDBj:1d7w
PDBsum1d7w
PubMed11705390
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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