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Yorodumi- PDB-1mhl: CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C CRYSTALLIZED... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mhl | |||||||||
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Title | CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C CRYSTALLIZED IN SPACE GROUP P2(1) AT PH 5.5 AND 20 DEG C | |||||||||
Components | (MYELOPEROXIDASE) x 2 | |||||||||
Keywords | MYELOPEROXIDASE | |||||||||
Function / homology | Function and homology information myeloperoxidase / hypochlorous acid biosynthetic process / Events associated with phagocytolytic activity of PMN cells / phagocytic vesicle lumen / response to gold nanoparticle / response to yeast / respiratory burst involved in defense response / low-density lipoprotein particle remodeling / response to food / azurophil granule ...myeloperoxidase / hypochlorous acid biosynthetic process / Events associated with phagocytolytic activity of PMN cells / phagocytic vesicle lumen / response to gold nanoparticle / response to yeast / respiratory burst involved in defense response / low-density lipoprotein particle remodeling / response to food / azurophil granule / removal of superoxide radicals / defense response to fungus / response to mechanical stimulus / peroxidase activity / hydrogen peroxide catabolic process / secretory granule / defense response / azurophil granule lumen / heparin binding / response to oxidative stress / response to lipopolysaccharide / lysosome / defense response to bacterium / intracellular membrane-bounded organelle / chromatin binding / heme binding / Neutrophil degranulation / negative regulation of apoptotic process / extracellular space / extracellular exosome / extracellular region / nucleoplasm / metal ion binding / nucleus Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.25 Å | |||||||||
Authors | Fenna, R.E. / Zeng, J. / Davey, C. | |||||||||
Citation | Journal: Arch.Biochem.Biophys. / Year: 1995 Title: Structure of the green heme in myeloperoxidase. Authors: Fenna, R. / Zeng, J. / Davey, C. #1: Journal: J.Mol.Biol. / Year: 1992 Title: X-Ray Crystal Structure of Canine Myeloperoxidase at 3 Angstroms Resolution Authors: Zeng, J. / Fenna, R.E. | |||||||||
History |
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Remark 650 | HELIX HELIX DETERMINATION METHOD: INSPECTION |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mhl.cif.gz | 248.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mhl.ent.gz | 201.9 KB | Display | PDB format |
PDBx/mmJSON format | 1mhl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/1mhl ftp://data.pdbj.org/pub/pdb/validation_reports/mh/1mhl | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO C 124 / 2: CIS PROLINE - PRO C 355 3: ASN C 549 - ASN C 550 OMEGA = 0.34 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: CIS PROLINE - PRO C 558 / 5: CIS PROLINE - PRO D 124 / 6: CIS PROLINE - PRO D 355 7: ASN D 549 - ASN D 550 OMEGA = 0.88 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 8: CIS PROLINE - PRO D 558 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.594, 0.6998, -0.3968), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 1 .. A 104 B 1 .. B 104 0.245 M1 C 113 .. C 578 D 113 .. D 578 0.244 MOLECULAR DYAD WITH SPHERICAL POLAR ANGLES: PSI = -63.872 DEG., PHI = 59.878 DEG., KAPPA = 180.0 DEG. | |
-Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | Mass: 12331.849 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: ISOFORM C / Source: (natural) Homo sapiens (human) / Cell: NEUTROPHIL / Organelle: AZUROPHIL GRANULES / Tissue: BLOOD / References: UniProt: P05164, peroxidase #2: Protein | Mass: 53218.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: ISOFORM C / Source: (natural) Homo sapiens (human) / Cell: NEUTROPHIL / Organelle: AZUROPHIL GRANULES / Tissue: BLOOD / References: UniProt: P05164, peroxidase |
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-Sugars , 2 types, 6 molecules
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 427 molecules
#5: Chemical | #6: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.06 % |
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Crystal grow | pH: 5.5 / Details: pH 5.5 |
Crystal grow | *PLUS Method: batch method |
Components of the solutions | *PLUS Conc.: 20 %(w/v) / Common name: PEG4000 / Details: or PEG6000 |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 Å |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: May 4, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 60087 / % possible obs: 88.5 % / Observed criterion σ(I): 1.7 / Redundancy: 3.7 % / Rmerge(I) obs: 0.059 |
-Processing
Software |
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Refinement | Resolution: 2.25→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 20.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→8 Å
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Refine LS restraints |
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