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Yorodumi- PDB-1gl7: Plasmid coupling protein TrwB in complex with the non-hydrolisabl... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gl7 | ||||||
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Title | Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP. | ||||||
Components | CONJUGAL TRANSFER PROTEIN TRWB | ||||||
Keywords | COUPLING PROTEIN / TYPE IV SECRETION SYSTEM CONJUGATIVE COUPLING PROTEIN FROM PLASMID | ||||||
Function / homology | Function and homology information nucleotide binding / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Gomis-Ruth, F.X. / Moncalian, G. / De La cruz, F. / Coll, M. | ||||||
Citation | Journal: Nature / Year: 2001 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gl7.cif.gz | 487.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gl7.ent.gz | 401.1 KB | Display | PDB format |
PDBx/mmJSON format | 1gl7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gl7_validation.pdf.gz | 793.5 KB | Display | wwPDB validaton report |
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Full document | 1gl7_full_validation.pdf.gz | 892.5 KB | Display | |
Data in XML | 1gl7_validation.xml.gz | 62.8 KB | Display | |
Data in CIF | 1gl7_validation.cif.gz | 89.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gl/1gl7 ftp://data.pdbj.org/pub/pdb/validation_reports/gl/1gl7 | HTTPS FTP |
-Related structure data
Related structure data | 1e9rSC 1e9sC 1gkiC 1gl6C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 48671.469 Da / Num. of mol.: 6 / Fragment: CYTOSOLIC FRAGMENT, RESIDUES 71-507 / Mutation: YES Source method: isolated from a genetically manipulated source Details: COMPLEX WITH ADPNP. / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q04230 #2: Chemical | ChemComp-ANP / #3: Chemical | ChemComp-CL / | #4: 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: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 1.05 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 |
Reflection | Resolution: 2.91→52 Å / Num. obs: 67095 / % possible obs: 90 % / Redundancy: 3.5 % / Biso Wilson estimate: 61 Å2 / Rmerge(I) obs: 0.107 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 2.91→3.07 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.453 / Mean I/σ(I) obs: 1.6 / % possible all: 66 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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. SAME INDICES AS IN 1GKI AND 1E9R USED. THERE IS NCS IN THE A.U. THE SIX PROTEIN CHAINS (A-G) ARE CHEMICALLY IDENTICAL. SOME N- AND C- ...Details: FREE RFACTOR USED UNTIL PENULTIMATE REFINEMENT CYCLE. SAME INDICES AS IN 1GKI AND 1E9R USED. 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: 64.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→50 Å
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Refine LS restraints |
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