Structure of PDB 3zs0 Chain D

Receptor sequence
>3zs0D (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA
3D structure
PDB3zs0 2-Thioxanthines are Mechanism-Based Inactivators of Myeloperoxidase that Block Oxidative Stress During Inflammation.
ChainD
Resolution2.3 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 ZS0 D P145 F407 P33 F295 BindingDB: IC50=2e+2nM
BS03 HEM D E242 M243 R333 H336 I339 F407 L417 R424 E130 M131 R221 H224 I227 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

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Molecular Function
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Biological Process
External links
PDB RCSB:3zs0, PDBe:3zs0, PDBj:3zs0
PDBsum3zs0
PubMed21880720
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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