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- PDB-1dot: CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dot | ||||||
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Title | CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION | ||||||
![]() | DUCK OVOTRANSFERRIN | ||||||
![]() | IRON TRANSPORT PROTEIN | ||||||
Function / homology | ![]() recycling endosome / iron ion transport / antibacterial humoral response / early endosome / extracellular space / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Rawas, A. / Muirhead, H. | ||||||
![]() | ![]() Title: Structure of diferric duck ovotransferrin at 2.35 A resolution. Authors: Rawas, A. / Muirhead, H. / Williams, J. #1: ![]() Title: Preliminary Crystallographic Studies on Duck Ovotransferrin Authors: Rawas, A. / Moreton, K. / Muirhead, H. / Williams, J. #2: ![]() Title: Molecular Structure of Serum Transferrin at 3.3 Angstroms Resolution Authors: Bailey, S. / Evans, R.W. / Garratt, R.C. / Gorinsky, B. / Hasnain, S. / Horsburgh, C. / Jhoti, H. / Lindley, P.F. / Mydin, A. / Sarra, R. / Watson, J.L. #3: ![]() Title: Structure of Human Lactoferrin at 3.2 Angstroms Resolution Authors: Anderson, B.F. / Baker, H.M. / Dodson, E.J. / Norris, G.E. / Rumball, S.V. / Waters, J.M. / Baker, E.N. | ||||||
History |
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Remark 700 | SHEET SHEETS N1, N2, C1, AND C2 ARE MIXED BETA SHEETS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 154.2 KB | Display | ![]() |
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PDB format | ![]() | 118.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.8 KB | Display | ![]() |
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Full document | ![]() | 499.2 KB | Display | |
Data in XML | ![]() | 24.3 KB | Display | |
Data in CIF | ![]() | 35.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: PRO 2 - PRO 3 OMEGA = 149.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: PRO 3 - LYS 4 OMEGA = 132.22 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: CIS PROLINE - PRO 71 4: THR 279 - SER 280 OMEGA = 300.70 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: LYS 344 - ILE 345 OMEGA = 127.92 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 75731.805 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Sugars , 2 types, 3 molecules ![](data/chem/img/NAG.gif)
![](data/chem/img/FUC.gif)
![](data/chem/img/FUC.gif)
#2: Sugar | #3: Sugar | ChemComp-FUC / | |
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-Non-polymers , 3 types, 322 molecules ![](data/chem/img/FE.gif)
![](data/chem/img/CO3.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CO3.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.88 % | ||||||||||||||||||||
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Crystal | *PLUS Density % sol: 48 % | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 291 K / pH: 5.8 / Method: batch method | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Detector: FILM / Date: 1986 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Num. obs: 29846 / % possible obs: 90 % / Rmerge(I) obs: 0.059 |
Reflection | *PLUS Highest resolution: 2.35 Å / Lowest resolution: 10 Å / Rmerge(I) obs: 0.059 |
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Processing
Software |
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Refinement | Resolution: 2.35→10 Å / σ(F): 1
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Displacement parameters | Biso mean: 28.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.35→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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