BioLiP

Structure of PDB 4dl1 Chain L

Receptor sequence

>4dl1L (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]

VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRN
QINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLP
FDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLAT
ELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLS
RVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMR
IGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLAR
KLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFV
NCSTLPALNLASWREA

3D structure

PDB

4dl1 Deconstruction of activity-dependent covalent modification of heme in human neutrophil myeloperoxidase by multistage mass spectrometry (MS(4)).

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	T168 F170 D172 S174 R239 E242 H336
Catalytic site (residue number reindexed from 1)	T56 F58 D60 S62 R127 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)
BS01	MAN	L	F439 K505	F327 K393
BS02	HEM	L	E242 M243 F332 R333 G335 H336 I339 L417 R424	E130 M131 F220 R221 G223 H224 I227 L305 R312
BS03	CA	L	T168 F170 D172 S174	T56 F58 D60 S62

Gene Ontology

	Molecular Function
GO:0004601	peroxidase activity
GO:0020037	heme binding

	Biological Process
GO:0006979	response to oxidative stress

View graph for
Molecular Function

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Biological Process

PDB	RCSB:4dl1, PDBe:4dl1, PDBj:4dl1
PDBsum	4dl1
PubMed	22352991
UniProt	P05164\|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)