+Open data
-Basic information
Entry | Database: PDB / ID: 1l7v | ||||||
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Title | Bacterial ABC Transporter Involved in B12 Uptake | ||||||
Components |
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Keywords | TRANSPORT PROTEIN/HYDROLASE / ABC transporter / integral membrane protein / ATP binding cassette / ATP hydrolysis / Vitamin B12 / TRANSPORT PROTEIN-HYDROLASE COMPLEX | ||||||
Function / homology | Function and homology information BtuCD complex / ABC-type vitamin B12 transporter / cobalamin transport complex / ABC-type vitamin B12 transporter activity / cobalamin transport / extrinsic component of membrane / ATPase-coupled transmembrane transporter activity / transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / ATP hydrolysis activity ...BtuCD complex / ABC-type vitamin B12 transporter / cobalamin transport complex / ABC-type vitamin B12 transporter activity / cobalamin transport / extrinsic component of membrane / ATPase-coupled transmembrane transporter activity / transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.2 Å | ||||||
Authors | Locher, K.P. / Lee, A.T. / Rees, D.C. | ||||||
Citation | Journal: Science / Year: 2002 Title: The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Authors: Locher, K.P. / Lee, A.T. / Rees, D.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1l7v.cif.gz | 214.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1l7v.ent.gz | 180.1 KB | Display | PDB format |
PDBx/mmJSON format | 1l7v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l7/1l7v ftp://data.pdbj.org/pub/pdb/validation_reports/l7/1l7v | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | Asymmetric unit contains full transporter: two copies each of BtuC and BtuD |
-Components
#1: Protein | Mass: 35487.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: BTUC / Production host: Escherichia coli (E. coli) / References: UniProt: P06609 #2: Protein | Mass: 27536.234 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: BTUD / Production host: Escherichia coli (E. coli) / References: UniProt: P06611, EC: 3.6.3.33 #3: Chemical | |
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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: 3.7 Å3/Da / Density % sol: 66.72 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 278 K / Method: vapor diffusion, sitting drop / pH: 8 Details: PEG 2000, LDAO, Tris, magnesium nitrate, MPD, D2O, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1.7712 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 18, 2001 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.7712 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→30 Å / Num. all: 30814 / Num. obs: 30660 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 3.2→3.29 Å / % possible all: 94.3 |
Reflection | *PLUS Lowest resolution: 30 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.067 |
Reflection shell | *PLUS % possible obs: 94.3 % / Rmerge(I) obs: 0.448 / Mean I/σ(I) obs: 4.1 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 3.2→15 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.2→15 Å
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Refinement | *PLUS Lowest resolution: 15 Å / Rfactor obs: 0.262 / Rfactor Rfree: 0.286 / Rfactor Rwork: 0.262 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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