[English] 日本語
Yorodumi- PDB-1tdw: Crystal structure of double truncated human phenylalanine hydroxy... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tdw | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU mutant A313T. | ||||||
Components | Phenylalanine-4-hydroxylase | ||||||
Keywords | OXIDOREDUCTASE / phenylalanine catabolism | ||||||
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 / Difference fourier / Resolution: 2.1 Å | ||||||
Authors | Erlandsen, H. / Pey, A.L. / Gamez, A. / Perez, B. / Desviat, L.R. / Aguado, C. / Koch, R. / Surendran, S. / Tyring, S. / Matalon, R. ...Erlandsen, H. / Pey, A.L. / Gamez, A. / Perez, B. / Desviat, L.R. / Aguado, C. / Koch, R. / Surendran, S. / Tyring, S. / Matalon, R. / Scriver, C.R. / Ugarte, M. / Martinez, A. / Stevens, R.C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2004 Title: Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Authors: Erlandsen, H. / Pey, A.L. / Gamez, A. / Perez, B. / Desviat, L.R. / Aguado, C. / Koch, R. / Surendran, S. / Tyring, S. / Matalon, R. / Scriver, C.R. / Ugarte, M. / Martinez, A. / Stevens, R.C. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1tdw.cif.gz | 80.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1tdw.ent.gz | 58.2 KB | Display | PDB format |
PDBx/mmJSON format | 1tdw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/td/1tdw ftp://data.pdbj.org/pub/pdb/validation_reports/td/1tdw | HTTPS FTP |
---|
-Related structure data
Related structure data | 1tg2C 1pahS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | molecule is a dimer (see 1PAH) |
-Components
#1: Protein | Mass: 35730.543 Da / Num. of mol.: 1 / Fragment: Delta NH 102 - Delta COOH 428 / Mutation: A313T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PAH / Plasmid: pMALc2 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P00439, phenylalanine 4-monooxygenase |
---|---|
#2: Chemical | ChemComp-FE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 60.04 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 5-10% Ethylene Glycol, 20-40 mM Pipes, pH 6.8, 8-15% PEG 2000, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 277 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-D / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Mar 12, 2003 / Details: Osmic Mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 184980 / Num. obs: 26608 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.5 % / Rmerge(I) obs: 0.118 / Net I/σ(I): 20 |
Reflection shell | Resolution: 2.1→2.17 Å / Redundancy: 4 % / Rmerge(I) obs: 0.612 / Mean I/σ(I) obs: 20 / Num. unique all: 2624 / % possible all: 100 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: Difference fourier Starting model: PDB entry 1pah Resolution: 2.1→19.93 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.1 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→19.93 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.1→2.23 Å / Rfactor Rfree error: 0.021
|