1MYP Myeloperoxidase date Apr 15, 1992
authors J.Zeng, R.E.Fenna
compound source
Myeloperoxidase (E.C.1.11.1.7)
Dog (Canis Familiaris)
symmetry Space Group: P 41 21 2
R_factor 0.257
crystal
cell
length a length b length c angle alpha angle beta angle gamma
133.000 133.000 203.600 90.00 90.00 90.00
method X-Ray Diffractionresolution 3.0 Å
ligand HEM, CA, NAGenzyme Peroxidase. Myeloperoxidase. Lactoperoxidase. Verdoperoxidase. Guaiacol peroxidase. Thiocyanate peroxidase. Eosinophil peroxidase. Japanese radish peroxidase. Horseradish peroxidase (HRP). Extensin peroxidase. Heme peroxidase. MPO. Oxyperoxidase. Protoheme peroxidase. Pyrocatechol peroxidase. Scopoletin peroxidase. Oxidoreductase E.C.1.11.1.7
related structures by homologous chain: 1MHL
similarity Belongs to the peroxidase family. Xpo subfamily.[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.
genes PNC1 (A. hypogaea); AT5G06720, MPH15.8, P53, PER53 (A. thaliana); HPRC1, HRPA2, PRXC1A (A. rusticana); CIP1 (C. cinereus); MPO (H. sapiens); MNP1 (P. chrysosporium)
function 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. It is responsible for microbicidal activity against a wide range of organisms. 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 referenceX-ray crystal structure of canine myeloperoxidase at 3 A resolution., Zeng J, Fenna RE, J Mol Biol 1992 Jul 5;226(1):185-207. PMID:1320128
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (203 Kb) [Save to disk]
  • Biological Unit Coordinates (1myp.pdb1.gz) 160 Kb
  • LPC: Ligand-Protein Contacts for 1MYP
  • CSU: Contacts of Structural Units for 1MYP
  • Likely Quarternary Molecular Structure file(s) for 1MYP
  • Retrieve 1MYP in mmCIF format [Save to disk]
  • View 1MYP in 3D
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  • Topology of domains/folds: Chain: A, Chain: B, Chain: C, Chain: D from TOPS (The Atlas of protein topology cartoons )
  • Structure-derived information
  • Dipole moment, from Dipole Server at Weizmann Institute
  • Crystal Contacts, from CryCo at Weizmann Institute
  • Genome occurence of 1MYP's fold from GeneCensus
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1myp.1, region A:,C [Jmol] [rasmolscript] [script source]
        - Domain d1myp.2, region B:,D [Jmol] [rasmolscript] [script source]
  • Fold representative 1myp from FSSP and Dali (Families of Structurally Similar Proteins)
  • Domain Definition for 1myp from 3Dee ( The Database of Protein Domain Definitions )
  • Class (fold), Architecture (subfold), Topology, Homologous superfamily: CATH
  • Summaries and structural analyses of PDB data files: PDBSum
  • Identification of Protein Pockets & Cavities at CASTp
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1myp_A] [1myp_B] [1myp_C] [1myp_D]
  • Other resources with information on 1MYP
  • InterPro: IPR002007 , IPR002016
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  • MMDB (Entrez's Structure Database)
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