Structure of PDB 6wxz Chain E

Receptor sequence
>6wxzE (length=465) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWRE
3D structure
PDB6wxz Discovery and structure activity relationships of 7-benzyl triazolopyridines as stable, selective, and reversible inhibitors of myeloperoxidase.
ChainE
Resolution2.226 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 E F439 K505 F327 K393
BS02 CA E T168 F170 D172 S174 T56 F58 D60 S62
BS03 HEC E E242 M243 T329 F332 R333 G335 H336 I339 L406 F407 L417 R424 E130 M131 T217 F220 R221 G223 H224 I227 L294 F295 L305 R312
BS04 UEY E T238 R239 E242 F366 M411 T126 R127 E130 F254 M299 MOAD: ic50=141nM
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:6wxz, PDBe:6wxz, PDBj:6wxz
PDBsum6wxz
PubMed33007547
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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