Structure of PDB 5mfa Chain A

Receptor sequence
>5mfaA (length=588) Species: 9606 (Homo sapiens) [Search protein sequence]
GCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDG
FSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWG
QLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQ
ADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNM
SNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRS
SEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQI
ITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQ
PFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAK
LNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFC
GLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGR
VGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDN
TGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREA
3D structure
PDB5mfa Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q257 D260 H261 D262 T334 F336 D338 S340 R405 E408 H502
Catalytic site (residue number reindexed from 1) Q101 D104 H105 D106 T178 F180 D182 S184 R249 E252 H346
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 A F369 Q370 F213 Q214
BS02 HEM A M253 G256 Q257 D260 D264 F265 T266 E408 M409 T495 R499 G501 H502 F573 L583 R590 M97 G100 Q101 D104 D108 F109 T110 E252 M253 T339 R343 G345 H346 F417 L427 R434
BS03 CA A D262 T334 F336 D338 S340 D106 T178 F180 D182 S184
Gene Ontology
Molecular Function
GO:0003682 chromatin binding
GO:0004601 peroxidase activity
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0001878 response to yeast
GO:0002149 hypochlorous acid biosynthetic process
GO:0002679 respiratory burst involved in defense response
GO:0006952 defense response
GO:0006979 response to oxidative stress
GO:0009612 response to mechanical stimulus
GO:0019430 removal of superoxide radicals
GO:0032094 response to food
GO:0032496 response to lipopolysaccharide
GO:0034374 low-density lipoprotein particle remodeling
GO:0042742 defense response to bacterium
GO:0042744 hydrogen peroxide catabolic process
GO:0043066 negative regulation of apoptotic process
GO:0050832 defense response to fungus
GO:1990268 response to gold nanoparticle
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005764 lysosome
GO:0030141 secretory granule
GO:0035578 azurophil granule lumen
GO:0042582 azurophil granule
GO:0043231 intracellular membrane-bounded organelle
GO:0070062 extracellular exosome
GO:0097013 phagocytic vesicle lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5mfa, PDBe:5mfa, PDBj:5mfa
PDBsum5mfa
PubMed28348079
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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