+Open data
-Basic information
Entry | Database: PDB / ID: 1ecp | ||||||
---|---|---|---|---|---|---|---|
Title | PURINE NUCLEOSIDE PHOSPHORYLASE | ||||||
Components | PURINE NUCLEOSIDE PHOSPHORYLASE | ||||||
Keywords | PENTOSYLTRANSFERASE / PURINE NUCLEOSIDE PHOSPHORYLASE / GLYCOSYLTRANSFERASE | ||||||
Function / homology | Function and homology information purine nucleoside interconversion / guanosine phosphorylase activity / purine-nucleoside phosphorylase / purine-nucleoside phosphorylase activity / purine nucleoside catabolic process / DNA damage response / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Mao, C. / Ealick, S.E. | ||||||
Citation | Journal: Structure / Year: 1997 Title: The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Authors: Mao, C. / Cook, W.J. / Zhou, M. / Koszalka, G.W. / Krenitsky, T.A. / Ealick, S.E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1ecp.cif.gz | 271.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1ecp.ent.gz | 221.7 KB | Display | PDB format |
PDBx/mmJSON format | 1ecp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ecp_validation.pdf.gz | 392.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1ecp_full_validation.pdf.gz | 417.8 KB | Display | |
Data in XML | 1ecp_validation.xml.gz | 29.2 KB | Display | |
Data in CIF | 1ecp_validation.cif.gz | 46.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ec/1ecp ftp://data.pdbj.org/pub/pdb/validation_reports/ec/1ecp | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 25850.748 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Plasmid: PBR322-DEO / Gene (production host): DEO OPERON / Production host: Escherichia coli (E. coli) / Strain (production host): BAU-1 References: UniProt: P0ABP8, purine-nucleoside phosphorylase #2: Water | ChemComp-HOH / | Source details | MOLECULE_NAME: PURINE NUCLEOSIDE PHOSPHORYLASE. THE PROTEIN WAS PURCHASED FROM SIGMA CO. THE ...MOLECULE_NAME: PURINE NUCLEOSIDE | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.38 % | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal | *PLUS Density % sol: 45 % | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 5 / PH range high: 4.8 | |||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction source | Wavelength: 1.5418 |
---|---|
Detector | Type: XUONG-HAMLIN MULTIWIRE MARK II / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 71593 / % possible obs: 70 % / Observed criterion σ(I): 1 / Redundancy: 3.26 % / Rmerge(I) obs: 0.0875 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 70600 / Num. measured all: 230200 / Rmerge(I) obs: 0.087 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2→15 Å / σ(F): 2 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|