Structure of PDB 7lae Chain E

Receptor sequence
>7laeE (length=465) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWRE
3D structure
PDB7lae Small molecule and macrocyclic pyrazole derived inhibitors of myeloperoxidase (MPO).
ChainE
Resolution2.97 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 E242 H336
Catalytic site (residue number reindexed from 1) T56 F58 D60 S62 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 BMA E F439 C497 F327 C385
BS02 MAN E F439 K505 F327 K393
BS03 HEM E E242 M243 T329 F332 R333 H336 I339 L417 R424 E130 M131 T217 F220 R221 H224 I227 L305 R312
BS04 CA E T168 F170 D172 S174 T56 F58 D60 S62
BS05 XRV E R239 E242 F366 R127 E130 F254
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:7lae, PDBe:7lae, PDBj:7lae
PDBsum7lae
PubMed33811992
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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