1DNU Oxidoreductase date Dec 16, 1999
title Structural Analyses Of Human Myeloperoxidase-Thiocyanate Complex
authors M.Blair-Johnson, T.Fiedler, R.Fenna
compound source
Molecule: Myeloperoxidase
Chain: A, B
Fragment: Myeloperoxidase Light Chain Containing Residues To 104;
Ec: 1.11.1.7
 Organism_scientific: Homo Sapiens
Organism_common: Human
Tissue: Blood
Cell: Neutrophil

Molecule: Myeloperoxidase
Chain: C, D
Fragment: Myeloperoxidase Heavy Chain Containing Residues 113 To 578;
Ec: 1.11.1.7
Organism_scientific: Homo Sapiens
Organism_common: Human
Tissue: Blood
Cell: Neutrophil
symmetry Space Group: P 1 21 1
R_factor 0.178
crystal
cell
length a length b length c angle alpha angle beta angle gamma
111.240 63.870 92.620 90.00 97.54 90.00
method X-Ray Diffractionresolution 1.85 Å
ligand CEA, NAG, MAN, FUC, CA, SCN, SO4, HEM, ACYenzyme Oxidoreductase E.C.1.11.1.7
related structures by homologous chain: 1CXP, 1D5L
similarity Xpo subfamily. Belongs to the peroxidase family.[An_peroxidase]
subunit Tetramer of two light chains and two heavy chains.
catalytic activ. Donor + h(2)o(2) = oxidized donor + 2 h(2)o. Cl(-) + h(2)o(2) = hocl + 2 h(2)o.
subcellular loc. Lysosomal.
gene MPO (H. sapiens)
function It is responsible for microbicidal activity against a wide range of organisms. In the stimulated pmn, mpo catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance pmn microbicidal activity. Part of the host defense system of polymorphonuclear leukocytes.
Gene
Ontology 		chain A: GO:0003682, GO:0004601, GO:0005509, GO:0005634, GO:0005764, GO:0006916, GO:0006952, GO:0006979, GO:0016491
chain B: GO:0003682, GO:0004601, GO:0005509, GO:0005634, GO:0005764, GO:0006916, GO:0006952, GO:0006979, GO:0016491
chain C: GO:0003682, GO:0004601, GO:0005509, GO:0005634, GO:0005764, GO:0006916, GO:0006952, GO:0006979, GO:0016491
chain D: GO:0003682, GO:0004601, GO:0005509, GO:0005634, GO:0005764, GO:0006916, GO:0006952, GO:0006979, GO:0016491
disease Alzheimer disease,susceptibility to
Myeloperoxidase deficiency
Mpd is an autosomal recessive defect that results in disseminated candidiasis. Defects in mpo are the cause of myeloperoxidase deficiency (mpd) [mim. 254600].
Primary referenceHuman 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, Biochemistry 2001 Nov 20;40(46):13990-7. PMID:11705390
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (231 Kb) [Save to disk]
  • Biological Unit Coordinates (1dnu.pdb1.gz) 208 Kb
  • LPC: Ligand-Protein Contacts for 1DNU
  • CSU: Contacts of Structural Units for 1DNU
  • Likely Quarternary Molecular Structure file(s) for 1DNU
  • Structure Factors (r1dnusf.ent.Z) 824 Kb
  • Retrieve 1DNU in mmCIF format [Save to disk]
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  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1dnu.1, region A:,C [Jmol] [rasmolscript] [script source]
        - Domain d1dnu.2, region B:,D [Jmol] [rasmolscript] [script source]
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  • SWISS-PROT database: [P05164] [Q14862]
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  • Conserved protein region description, domain view and alignment from family An_peroxidase (PF03098) of Pfam.
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