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Open data
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Basic information
Entry | Database: PDB / ID: 1gki | ||||||
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Title | Plasmid coupling protein TrwB in complex with ADP and Mg2+. | ||||||
![]() | CONJUGAL TRANSFER PROTEIN TRWB | ||||||
![]() | COUPLING PROTEIN / BACTERIAL CONJUGATION / F1-ATPASE-LIKE QUATERNARY STRUCTURE / RING HELICASES | ||||||
Function / homology | ![]() nucleotide binding / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gomis-Ruth, F.X. / Moncalian, G. / De La cruz, F. / Coll, M. | ||||||
![]() | ![]() Title: The Bacterial Conjugation Protein Trwb Resembles Ring Helicases and F1-ATPase Authors: Gomis-Ruth, F.X. / Moncalian, G. / Perez-Luque, R. / Gonzalez, A. / Cabezon, E. / De La Cruz, F. / Coll, M. #1: Journal: J.Biol.Chem. / Year: 2002 Title: Conjugative Plasmid Protein Trwb, an Integral Membrane Type Iv Secretion System Coupling Protein: Detailed Structural Features and Mapping of the Active Site Cleft. Authors: Gomis-Ruth, F. / Moncalian, G. / De La Cruz, F. / Coll, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 496.7 KB | Display | ![]() |
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PDB format | ![]() | 407.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1e9rSC ![]() 1e9sC ![]() 1gl6C ![]() 1gl7C 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: 48671.469 Da / Num. of mol.: 6 / Fragment: CYTOSOLIC, RESIDUES 71-507 / Mutation: YES Source method: isolated from a genetically manipulated source Details: COMPLEX WITH ADP AND MG2+. / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ADP / #3: Chemical | ChemComp-MG / #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | CHAIN A, B, D, E, F, G FIRST 70 RESIDUES DELETED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57 % |
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Crystal grow | pH: 7.5 / Details: pH 7.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 3→51.3 Å / Num. obs: 67169 / % possible obs: 100 % / Redundancy: 5.4 % / Biso Wilson estimate: 66.6 Å2 / Rmerge(I) obs: 0.118 / Net I/σ(I): 5.9 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.418 / Mean I/σ(I) obs: 1.5 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1E9R Resolution: 3→50 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: FREE RFACTOR USED UNTIL PENULTIMATE REFINEMENT CYCLE. THERE IS NCS IN THE A.U. THE SIX PROTEIN CHAINS (A-G) ARE CHEMICALLY IDENTICAL. SOME N- AND C-TERMINAL RESIDUES ARE DISORDERED AND HAVE NOT BEEN TRACED.
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Displacement parameters | Biso mean: 49.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→50 Å
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Refine LS restraints |
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