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Open data
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Basic information
Entry | Database: PDB / ID: 1b46 | ||||||
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Title | OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KPK | ||||||
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![]() | PEPTIDE BINDING PROTEIN / COMPLEX (PEPTIDE TRANSPORT-PEPTIDE) / PEPTIDE TRANSPORT | ||||||
Function / homology | ![]() peptide transport / peptide transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tame, J.R.H. / Sleigh, S.H. / Wilkinson, A.J. | ||||||
![]() | ![]() Title: Crystallographic and calorimetric analysis of peptide binding to OppA protein. Authors: Sleigh, S.H. / Seavers, P.R. / Wilkinson, A.J. / Ladbury, J.E. / Tame, J.R. #1: ![]() Title: The Role of Water in Sequence-Independent Ligand Binding by an Oligopeptide Transporter Protein Authors: Tame, J.R. / Sleigh, S.H. / Wilkinson, A.J. / Ladbury, J.E. #2: ![]() Title: The Crystal Structures of the Oligopeptide-Binding Protein Oppa Complexed with Tripeptide and Tetrapeptide Ligands Authors: Tame, J.R. / Dodson, E.J. / Murshudov, G. / Higgins, C.F. / Wilkinson, A.J. #3: ![]() Title: Structure Determination of Oppa at 2.3 Angstroms Resolution Using Multiple Wavelength Anomalous Methods Authors: Glover, I.D. / Denny, R. / Nguti, N.D. / Mcsweeney, S. / Thompson, A. / Dodson, E. / Wilkinson, A.J. / Tame, J.R.H. #4: ![]() Title: The Structural Basis of Sequence-Independent Peptide Binding by Oppa Protein Authors: Tame, J.R. / Murshudov, G.N. / Dodson, E.J. / Neil, T.K. / Dodson, G.G. / Higgins, C.F. / Wilkinson, A.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126.1 KB | Display | ![]() |
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PDB format | ![]() | 96.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b05C ![]() 1b32C ![]() 1b3fC ![]() 1b3gC ![]() 1b3lC ![]() 1b40C ![]() 1b4zC ![]() 1b51C ![]() 1b52C ![]() 1b58C ![]() 1b5iC ![]() 1b5jC ![]() 1b9jC ![]() 1qkaC ![]() 1qkbC ![]() 1olb S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 58878.984 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 373.490 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED | ||||
#3: Chemical | ChemComp-IUM / ![]() #4: Chemical | ChemComp-ACT / ![]() #5: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50 % / Description: FLASH COOLED TO 120K | |||||||||||||||||||||||||
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Crystal grow![]() | pH: 5.5 / Details: CO-CRYSTALLIZED WITH URANIUM ACETATE, PH 5.5 | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Wavelength: 1.54 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.75→15 Å / Num. obs: 59716 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Biso Wilson estimate: 26 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 5.4 |
Reflection shell | Resolution: 1.8→1.83 Å / Rmerge(I) obs: 0.365 / % possible all: 92.7 |
Reflection | *PLUS Rmerge(I) obs: 0.092 |
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Processing
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Refinement | Method to determine structure![]() Starting model: PDB ENTRY 1OLB ![]() 1olb Resolution: 1.8→15 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 30.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |