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Open data
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Basic information
Entry | Database: PDB / ID: 5jsz | |||||||||
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Title | Folate ECF transporter: apo state | |||||||||
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![]() | TRANSPORT PROTEIN / ECF transporter / folate / membrane protein / vitamin transport | |||||||||
Function / homology | ![]() Translocases / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / transmembrane transporter activity / ATPase-coupled transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Swier, L.J.Y.M. / Guskov, A. / Slotboom, D.J. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insight in the toppling mechanism of an energy-coupling factor transporter. Authors: Swier, L.J. / Guskov, A. / Slotboom, D.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 | ![]() | 795 KB | Display | ![]() |
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PDB format | ![]() | 663 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 507.8 KB | Display | ![]() |
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Full document | ![]() | 577.3 KB | Display | |
Data in XML | ![]() | 72.7 KB | Display | |
Data in CIF | ![]() | 97 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5d0yC ![]() 5d3mSC 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33166.418 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: 10 HIS-TAG AND TEV-CLEAVAGE SITE AT N-TERMINUS Source: (gene. exp.) ![]() Strain: ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778 Gene: ecfA1, cbiO1, Ldb0424 / Production host: ![]() ![]() References: UniProt: Q1GBJ0, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances #2: Protein | Mass: 31672.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778 Gene: ecfA2, cbiO2, Ldb0425 / Production host: ![]() ![]() References: UniProt: Q1GBI9, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances #3: Protein | Mass: 20483.604 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: STREPII TAG AT C-TERMINUS Source: (gene. exp.) ![]() Strain: ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778 Gene: Ldb1625 / Production host: ![]() ![]() #4: Protein | Mass: 30290.283 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: ecfT, AT236_00396, CFL1_00754, SB57_06620 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.16 Å3/Da / Density % sol: 61.02 % |
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Crystal grow | Temperature: 278 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 50MM TRIS, 17% PEG 350MME, 2% NG, 10MM SPERMIDINE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 28, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97242 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 52519 / % possible obs: 92.6 % / Redundancy: 1.76 % / Rmerge(I) obs: 0.043 / Net I/σ(I): 10.54 |
Reflection shell | Resolution: 3→3.08 Å / Redundancy: 1.72 % / % possible all: 86.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5D3M Resolution: 3.004→49.004 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 35
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.004→49.004 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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