Structure of PDB 6bmt Chain A

Receptor sequence
>6bmtA (length=573) Species: 9606 (Homo sapiens) [Search protein sequence]
TCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTP
GVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDF
TPEPAAGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPG
SNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQD
NGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLR
EHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTA
MRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEP
NPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRER
LFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVL
RNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRK
LRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSN
SYPRDFVNCSTLPALNLASWREA
3D structure
PDB6bmt Identification and structural characterization of a novel myeloperoxidase inhibitor from Staphylococcus delphini.
ChainA
Resolution2.403 Å
3D
structure
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Enzymatic activity
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 CA A D262 T334 F336 D338 S340 D97 T163 F165 D167 S169
BS02 HEM A M253 G256 Q257 D260 D264 F265 T266 E408 M409 T495 F498 R499 H502 F573 R590 M88 G91 Q92 D95 D99 F100 T101 E237 M238 T324 F327 R328 H331 F402 R419
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:6bmt, PDBe:6bmt, PDBj:6bmt
PDBsum6bmt
PubMed29524428
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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