+Open data
-Basic information
Entry | Database: PDB / ID: 2pah | ||||||
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Title | TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE | ||||||
Components | PROTEIN (PHENYLALANINE HYDROXYLASE) | ||||||
Keywords | HYDROXYLASE / PHENYLKETONURIA | ||||||
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: 3.1 Å | ||||||
Authors | Stevens, R.C. / Fusetti, F. / Erlandsen, H. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 Title: Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. Authors: Fusetti, F. / Erlandsen, H. / 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 | 2pah.cif.gz | 138.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2pah.ent.gz | 108.8 KB | Display | PDB format |
PDBx/mmJSON format | 2pah.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2pah_validation.pdf.gz | 433 KB | Display | wwPDB validaton report |
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Full document | 2pah_full_validation.pdf.gz | 457.4 KB | Display | |
Data in XML | 2pah_validation.xml.gz | 26.6 KB | Display | |
Data in CIF | 2pah_validation.cif.gz | 34.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pa/2pah ftp://data.pdbj.org/pub/pdb/validation_reports/pa/2pah | HTTPS FTP |
-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: 38641.926 Da / Num. of mol.: 2 / Fragment: RESIDUES 118-452 Source method: isolated from a genetically manipulated source Details: ACTIVE SITE IRON ATOM FE / Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET-3A-D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P00439, phenylalanine 4-monooxygenase #2: Chemical | |
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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: 3.36 Å3/Da / Density % sol: 60 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 0.6 M MGSO4, 0.2 M NAK TARTRATE, 10% PEG-4000, 0.1 M BIS-TRIS PROPANE (PH 7.0) | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 60 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1997 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→20 Å / Num. obs: 120922 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 6.5 % / Biso Wilson estimate: 33 Å2 / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 10 |
Reflection shell | Resolution: 3.1→3.2 Å / Redundancy: 2 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 2 / Rsym value: 0.25 / % possible all: 98 |
Reflection | *PLUS Num. obs: 18446 / Num. measured all: 120922 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1TOH Resolution: 3.1→20 Å / Data cutoff high absF: 100000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 33 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.1→3.2 Å / Total num. of bins used: 6 /
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 3.2 Å / Rfactor Rfree: 0.326 / % reflection Rfree: 10 % / Rfactor Rwork: 0.251 |