+Open data
-Basic information
Entry | Database: PDB / ID: 1abe | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN | |||||||||
Components | L-ARABINOSE-BINDING PROTEIN | |||||||||
Keywords | BINDING PROTEIN | |||||||||
Function / homology | Function and homology information L-arabinose transmembrane transport / ABC-type monosaccharide transporter activity / monosaccharide binding / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / carbohydrate binding / membrane Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | |||||||||
Authors | Vyas, N.K. / Quiocho, F.A. | |||||||||
Citation | Journal: Nature / Year: 1984 Title: Novel stereospecificity of the L-arabinose-binding protein Authors: Quiocho, F.A. / Vyas, N.K. #1: Journal: Nature / Year: 1989 Title: Substrate Specificity and Affinity of a Protein Modulated by Bound Water Molecules Authors: Quiocho, F.A. / Wilson, D.K. / Vyas, N.K. #2: Journal: J.Mol.Biol. / Year: 1974 Title: Crystallographic Data of an L-Arabinose-Binding Protein from Escherichia Coli Authors: Quiocho, F.A. / Phillips Jr., G.N. / Parsons, R.G. / Hogg, R.W. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1abe.cif.gz | 75.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1abe.ent.gz | 55.9 KB | Display | PDB format |
PDBx/mmJSON format | 1abe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1abe_validation.pdf.gz | 401 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1abe_full_validation.pdf.gz | 409.6 KB | Display | |
Data in XML | 1abe_validation.xml.gz | 8.6 KB | Display | |
Data in CIF | 1abe_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1abe ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1abe | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 33250.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P02924 |
---|---|
#2: Sugar | ChemComp-ARA / |
#3: Sugar | ChemComp-ARB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.21 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 6.5 / Method: microdialysisDetails: referred to 'Quiocho, F.A.', (1974) J.Mol.Biol., 86, 491-493 | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.7→8 Å /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 8 Å / Num. reflection obs: 26634 / σ(I): 3 / Rfactor obs: 0.137 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |