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BioLiP

Structure of PDB 4dl1 Chain O

Receptor sequence
>4dl1O (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA
3D structure
PDB4dl1 Deconstruction of activity-dependent covalent modification of heme in human neutrophil myeloperoxidase by multistage mass spectrometry (MS(4)).
ChainO
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R239
Catalytic site (residue number reindexed from 1) R127
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 O F439 K505 F327 K393
BS02 HEM O E242 M243 F332 R333 G335 H336 I339 L417 R424 E130 M131 F220 R221 G223 H224 I227 L305 R312
BS03 CA O T168 F170 D172 S174 T56 F58 D60 S62
BS04 0KY O R239 E242 F366 F407 R127 E130 F254 F295
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:4dl1, PDBe:4dl1, PDBj:4dl1
PDBsum4dl1
PubMed22352991
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

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