Brand  (β version)

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Code Name Style Show Link
BR Bromide ion
SO4 Sulfate ion
CYN Cyanide ion
ACT Acetate ion
HEM Protoporphyrin ix containing Fe
CA Calcium ion

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Non-standard Residues
Code Name Show
CSO S-hydroxycysteine
Glycosylation
Code Name Emphasize
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
BMA Beta-D-mannopyranose
MAN Alpha-D-mannopyranose
FUC Alpha-L-fucopyranose
Modification
Code Name Show
Code : 1D7W   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C COMPLEXED WITH CYANIDE AND BROMIDE AT PH 4.0
Release Data : 2001-12-12
Compound :
mol_id molecule chains
1 MYELOPEROXIDASE A,B
ec: 1.11.1.7
fragment: LIGHT CHAIN
mol_id molecule chains
2 MYELOPEROXIDASE C,D
ec: 1.11.1.7
fragment: HEAVY CHAIN
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
tissue: BLOOD
cell: NEUTROPHIL
mol_id organism_scientific organism_common
2 Homo sapiens  (taxid:9606) Human
tissue: BLOOD
cell: NEUTROPHIL
Authors : Fiedler, T.J., Fenna, R.E.
Keywords : HEME-PROTEIN, PEROXIDASE, OXIDOREDUCTASE, PEROXIDASE-CYANIDE-BROMIDE COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.

Blair-Johnson, M.,Fiedler, T.,Fenna, R.
(2001)  Biochemistry  40 : 13990 - 13997

PubMed: 11705390
DOI: 10.1021/bi0111808

Structure of the Green Heme in Myeloperoxidase

Fenna, R.,Zeng, J.,Davey, C.
(1995)  Arch.Biochem.Biophys.  316 : 653

DOI: 10.1006/abbi.1995.1086

2.3 Angstrom Resolution X-Ray Crystal Structure of the Bisubstrate Analogue Inhibitor Salicylhydroxamic Acid Bound to Human Myeloperoxidase: A Model for a Prereaction Complex with Hydrogen Peroxide

Davey, C.A.,Fenna, R.E.
(1996)  Biochemistry  35 : 10967

DOI: 10.1021/bi960577m

X-Ray Crystal Structure of Canine Myeloperoxidase at 3 Angstrom Resolution

Zeng, J.,Fenna, R.E.
(1992)  J.Mol.Biol.  226 : 185

Site-Directed Mutagenesis of Human Myeloperoxidase: Further Identification of Residues Involved in Catalytic Activity and Heme Interaction

Jacquet, A.,Garcia-Quintana, L.,Deleersnyder, V.  et al.
(1994)  Biochem.Biophys.Res.Commun.  202 : 73

DOI: 10.1006/bbrc.1994.1895

Chain : C, D
UniProt : P05164 (PERM_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
chloride + H2O2 + H(+) = hypochlorous acid + H2O 1.11.2.2 PubMed:16125131, PubMed:17074761, PubMed:17438335, PubMed:19608745, PubMed:21880720, PubMed:22131345, PubMed:22902565, PubMed:24194519, PubMed:9359420, PubMed:9922160
left-to-right PubMed:16125131, PubMed:17074761, PubMed:17438335, PubMed:19608745, PubMed:21880720, PubMed:22131345, PubMed:22902565, PubMed:24194519
thiocyanate + H2O2 + H(+) = hypothiocyanous acid + H2O - PubMed:16125131, PubMed:6295491
left-to-right
bromide + H2O2 = hypobromite + H2O - PubMed:16125131, PubMed:17438335
left-to-right
iodide + H2O2 = hypoiodite + H2O - PubMed:1318692
left-to-right
Cofactor: Evidence: Note:
Ca(2+) ECO:0000269 | PubMed:10766826
ECO:0000269 | PubMed:11705390
ECO:0000269 | PubMed:19608745
ECO:0000269 | PubMed:21880720
ECO:0000269 | PubMed:22352991
ECO:0000269 | PubMed:28348079
ECO:0000269 | PubMed:28808028
ECO:0000269 | PubMed:29306874
ECO:0000269 | PubMed:36150500
ECO:0000269 | PubMed:40963017
ECO:0000269 | PubMed:7840679
Binds 1 Ca(2+) ion per monomer.
heme b ECO:0000269 | PubMed:17438335
ECO:0000269 | PubMed:19608745
ECO:0000269 | PubMed:21880720
ECO:0000269 | PubMed:22352991
ECO:0000269 | PubMed:23843990
ECO:0000269 | PubMed:28348079
ECO:0000269 | PubMed:40963017
ECO:0000269 | PubMed:7840679
Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.