+Open data
-Basic information
Entry | Database: PDB / ID: 1qjq | |||||||||
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Title | FERRIC HYDROXAMATE RECEPTOR FROM ESCHERICHIA COLI (FHUA) | |||||||||
Components | FERRIC HYDROXAMATE RECEPTOR | |||||||||
Keywords | TONB DEPENDENT RECEPTOR / LIPOPOLYSACCHARIDE / FERRICHROME-IRON RECEPTOR / INTEGRAL OUTER MEMBRANE PROTEIN / TONB-DEPENDENT RECEPTOR / SIDEROPHORE RECEPTOR / ACTIVE TRANSPORT / IRON TRANSPORT / SIDEROPHORE-ANTIBIOTIC CONJUGATE | |||||||||
Function / homology | Function and homology information 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 | ESCHERICHIA COLI (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å | |||||||||
Authors | Ferguson, A.D. / Braun, V. / Fiedler, H.-P. / Coulton, J.W. / Diederichs, K. / Welte, W. | |||||||||
Citation | Journal: Protein Sci. / Year: 2000 Title: Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Authors: Ferguson, A.D. / Braun, V. / Fiedler, H.P. / Coulton, J.W. / Diederichs, K. / Welte, W. #1: 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. #2: Journal: Science / Year: 1998 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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qjq.cif.gz | 173.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qjq.ent.gz | 133.8 KB | Display | PDB format |
PDBx/mmJSON format | 1qjq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qjq_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 1qjq_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 1qjq_validation.xml.gz | 38.6 KB | Display | |
Data in CIF | 1qjq_validation.cif.gz | 54.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qj/1qjq ftp://data.pdbj.org/pub/pdb/validation_reports/qj/1qjq | HTTPS FTP |
-Related structure data
Related structure data | 1qkcC 1qffS C: citing same article (ref.) S: Starting model for refinement |
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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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Details | BIOLOGICAL_UNIT: MONOMER |
-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: A HEXAHISTIDINE TAG PLUS FIVE ADDITIONAL LINKER RESIDUES HAVE BEEN GENETICALLY INSERTED AFTER RESIDUE 405 OF THE MATURE FHUA SEQUENCE AS AN AFFINITY TAG Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Cell: BACTERIAL / Cellular location: OUTER MEMBRANE / Gene: FHUA / Variant: RA CHEMOTYPE / Plasmid: PHX405 / Cell (production host): BACTERIAL / Cellular location (production host): CYTOPLASM / Gene (production host): FHUA405.H6 / Production host: ESCHERICHIA COLI K-12 (bacteria) / Strain (production host): AW740 / Variant (production host): RA CHEMOTYPE / References: UniProt: P06971 |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D- ...alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose-(1-3)-[L-glycero-alpha-D-manno-heptopyranose-(1-7)]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-2,3-dideoxy-alpha-D-glucoyranose Source method: isolated from a genetically manipulated source |
-Non-polymers , 6 types, 407 molecules
#3: Chemical | ChemComp-FTT / #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-NI / | #7: Chemical | ChemComp-PFC / | #8: Water | ChemComp-HOH / | |
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-Details
Compound details | RESIDUES 406 - 416 RESULT FROM A HEXAHISTID |
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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: 4.6 Å3/Da / Density % sol: 74 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.4 Details: 100MM SODIUM CACODYLATE (PH 6.4), 14.5% PEG 2000 MONOMETHYLETHER, 20% GLYCEROL, 3% PEG 200, 1 MM PHENYLFERRICROCIN-IRON | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 8 / Method: vapor diffusion, hanging dropDetails: equal volume of protein and reservoir solution were used for the drop | ||||||||||||||||||||||||||||||||||||||||
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: MAX II / Beamline: I711 / Wavelength: 1.051 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 15, 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: 2.95→30 Å / Num. obs: 32078 / % possible obs: 94.8 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: -0.7 Å2 / Rmerge(I) obs: 0.064 / Rsym value: 0.062 / Net I/σ(I): 20.26 |
Reflection shell | Resolution: 2.95→2.99 Å / Rmerge(I) obs: 0.281 / Mean I/σ(I) obs: 4.03 / Rsym value: 0.251 / % possible all: 77.7 |
Reflection | *PLUS Num. obs: 31400 / Num. measured all: 231385 |
Reflection shell | *PLUS % possible obs: 82 % / Rmerge(I) obs: 0.291 / Mean I/σ(I) obs: 3.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1QFF Resolution: 2.95→50 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1210970.9 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 46.518 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 70.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.95→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.95→3.13 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.4 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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