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- PDB-1ldf: CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) MUTA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ldf | |||||||||
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Title | CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) MUTATION W48F, F200T | |||||||||
![]() | Glycerol uptake facilitator protein | |||||||||
![]() | TRANSPORT PROTEIN / GLYCEROL-CONDUCTING MEMBRANE CHANNEL PROTEIN | |||||||||
Function / homology | ![]() glycerol channel activity / glycerol transmembrane transporter activity / urea transmembrane transporter activity / glycerol transmembrane transport / cellular response to mercury ion / channel activity / membrane => GO:0016020 / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Nollert, P. / Miercke, L.J.W. / O'Connell, J. / Stroud, R.M. | |||||||||
![]() | ![]() Title: Control of the selectivity of the aquaporin water channel family by global orientational tuning. Authors: Tajkhorshid, E. / Nollert, P. / Jensen, M.O. / Miercke, L.J. / O'Connell, J. / Stroud, R.M. / Schulten, K. #1: ![]() Title: Structure of a Glycerol-Conducting Channel and the Basis for Its Selectivity Authors: Fu, D. / Libson, A. / Miercke, L.J. / Weitzman, C. / Nollert, P. / Krucinski, J. / Stroud, R.M. | |||||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.5 KB | Display | ![]() |
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PDB format | ![]() | 46.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.6 KB | Display | ![]() |
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Full document | ![]() | 442.1 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ldaC ![]() 1ldiC ![]() 1fx8S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is generated by the crystallographic four-fold axis: X,Y,Z; -X+1, -Y+1, Z; -Y+1,X, Z; Y,-X+1,Z |
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Components
#1: Protein | Mass: 29714.740 Da / Num. of mol.: 1 / Mutation: W48F, F200T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||
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#2: Sugar | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 66.41 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: GLPF AT 15-20 MG/ML, 28% (W/V) PEG 2000, 100 MM BICINE pH 9.5, 15 % (V/V) GLYCEROL, 35 MM, N-OCTYL-BETA-D-GLUCOSIDE, MGCL2, 5 MM DTT, pH 9.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.9 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC / Detector: CCD / Date: Nov 10, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→35 Å / Num. obs: 25710 / % possible obs: 97.9 % / Observed criterion σ(I): 0 / Redundancy: 4.786 % / Rmerge(I) obs: 0.085 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.1→2.18 Å / Rmerge(I) obs: 0.363 / % possible all: 89.6 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 35 Å / Num. measured all: 128187 / Rmerge(I) obs: 0.085 |
Reflection shell | *PLUS Rmerge(I) obs: 0.363 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FX8 Resolution: 2.1→35 Å / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2.1→35 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 35 Å / Rfactor obs: 0.23 / Rfactor Rfree: 0.243 / Rfactor Rwork: 0.23 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |