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Open data
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Basic information
Entry | Database: PDB / ID: 1qfg | |||||||||
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Title | E. COLI FERRIC HYDROXAMATE RECEPTOR (FHUA) | |||||||||
![]() | PROTEIN (FERRIC HYDROXAMATE UPTAKE RECEPTOR) | |||||||||
![]() | METAL TRANSPORT / TONB-DEPENDENT RECEPTOR / INTEGRAL OUTER MEMBRANE PROTEIN / FERRICHROME-IRON RECEPTOR / ACTIVE TRANSPORT / IRON TRANSPORT PROTEIN / LIPOPOLYSACCHARIDE | |||||||||
Function / homology | ![]() siderophore transmembrane transport / siderophore uptake transmembrane transporter activity / virion binding / toxic substance binding / transmembrane transporter complex / cell outer membrane / signaling receptor activity / intracellular iron ion homeostasis / iron ion binding / protein domain specific binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Ferguson, A.D. / Welte, W. / Hofmann, E. / Lindner, B. / Holst, O. / Coulton, J.W. / Diederichs, K. | |||||||||
![]() | ![]() Title: A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Authors: Ferguson, A.D. / Welte, W. / Hofmann, E. / Lindner, B. / Holst, O. / Coulton, J.W. / Diederichs, K. #1: ![]() Title: Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Authors: Ferguson, A.D. / Hofmann, E. / Coulton, J.W. / Diederichs, K. / Welte, W. #2: Journal: Protein Sci. / Year: 1998 Title: An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12. Authors: Ferguson, A.D. / Breed, J. / Diederichs, K. / Welte, W. / Coulton, J.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 162.8 KB | Display | ![]() |
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PDB format | ![]() | 131.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
-Protein / Sugars , 2 types, 2 molecules A
#1: Protein | Mass: 80051.109 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH LIPOPOLYSACCHARIDE / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose-(1-3)-L-glycero- ...alpha-D-glucopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2,3-dideoxy-alpha-D-glucoyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source |
-Non-polymers , 9 types, 266 molecules ![](data/chem/img/NI.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/FTT.gif)
![](data/chem/img/DAO.gif)
![](data/chem/img/MYR.gif)
![](data/chem/img/DDQ.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/FTT.gif)
![](data/chem/img/DAO.gif)
![](data/chem/img/MYR.gif)
![](data/chem/img/DDQ.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-NI / | ||||||||||||||
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#4: Chemical | #5: Chemical | ChemComp-FTT / #6: Chemical | ChemComp-DAO / | #7: Chemical | ChemComp-MYR / | #8: Chemical | #9: Chemical | #10: Chemical | ChemComp-GOL / #11: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.65 Å3/Da / Density % sol: 73.54 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.4 Details: 100MM SODIUM CACODYLATE (PH 6.4), 12.5% PEG 2000 MONOMETHYLETHER, 20% GLYCEROL, 1% CIS-INOSITOL, 3% PEG 200, VAPOR DIFFUSION, HANGING DROP, temperature 290K | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Details: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.051 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→42.3 Å / Num. obs: 53749 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 6.4 % / Biso Wilson estimate: 43.12 Å2 / Rmerge(I) obs: 0.078 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.45→2.5 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.334 / % possible all: 92.2 |
Reflection shell | *PLUS % possible obs: 92.2 % |
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Processing
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Refinement | Resolution: 2.5→42.3 Å / Rfactor Rfree error: 0.006 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Stereochemistry target values: MOD. ENGH&HUBER PROTEIN_REP.PARAM (CNS)
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.33 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 65.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→42.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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