Structure of PDB 5fiw Chain D

Receptor sequence
>5fiwD (length=464) Species: 9606 (Homo sapiens) [Search protein sequence]
NCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQ
INALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPF
DNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATE
LKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTY
RSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSR
VFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRI
GLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARK
LMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFW
WENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVN
CSTLPALNLASWRE
3D structure
PDB5fiw Crystal Structure of Human Myeloperoxidase at 1.7 Angstroms Resolution
ChainD
Resolution1.7 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) T55 F57 D59 S61 R126 E129 H223
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 HEM D E242 M243 R333 G335 H336 F407 L417 R424 E129 M130 R220 G222 H223 F294 L304 R311
BS02 BMA D F439 K505 F326 K392
BS03 CA D T168 F170 D172 S174 T55 F57 D59 S61
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:5fiw, PDBe:5fiw, PDBj:5fiw
PDBsum5fiw
PubMed
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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