+Open data
-Basic information
Entry | Database: PDB / ID: 1pah | ||||||
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Title | HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424 | ||||||
Components | PHENYLALANINE HYDROXYLASE | ||||||
Keywords | OXIDOREDUCTASE / PHENYLALANINE / HYDROXYLASE / PHENYLKETONURIA / PKU | ||||||
Function / homology | Function and homology information Phenylketonuria / Phenylalanine metabolism / phenylalanine 4-monooxygenase / phenylalanine 4-monooxygenase activity / tyrosine biosynthetic process / catecholamine biosynthetic process / L-phenylalanine catabolic process / amino acid biosynthetic process / iron ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Stevens, R.C. / Erlandsen, H. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1997 Title: Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Authors: Erlandsen, H. / Fusetti, F. / Martinez, A. / Hough, E. / Flatmark, T. / Stevens, R.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pah.cif.gz | 72.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pah.ent.gz | 55.7 KB | Display | PDB format |
PDBx/mmJSON format | 1pah.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pa/1pah ftp://data.pdbj.org/pub/pdb/validation_reports/pa/1pah | HTTPS FTP |
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-Related structure data
Related structure data | 1tohS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 35700.516 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Details: TRUNCATED FORM, DELTA COOH 1-102, DELTA NH 428-452 / Source: (gene. exp.) Homo sapiens (human) / Organ: LIVER / Organ (production host): LIVER / Production host: Escherichia coli (E. coli) / References: UniProt: P00439, phenylalanine 4-monooxygenase |
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#2: Chemical | ChemComp-FE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 62 % | ||||||||||||||||||||
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Crystal grow | pH: 6.8 / Details: pH 6.8 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Erlandsen, H., (1997) FEBS Lett., 406, 171. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM1A / Wavelength: 0.873 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1996 / Details: DUEL SLITS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 30932 / % possible obs: 99.7 % / Observed criterion σ(I): 2 / Redundancy: 5.9 % / Biso Wilson estimate: 23.3 Å2 / Rmerge(I) obs: 0.048 / Rsym value: 0.067 / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 4 % / Rmerge(I) obs: 0.39 / Mean I/σ(I) obs: 20 / Rsym value: 0.398 / % possible all: 99.1 |
Reflection | *PLUS Num. measured all: 18331 |
Reflection shell | *PLUS % possible obs: 99.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1TOH Resolution: 2→20 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 30.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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