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- PDB-1ccf: How an Epidermal Growth Factor (EGF)-Like Domain Binds Calcium-Hi... -
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Basic information
Entry | Database: PDB / ID: 1ccf | ||||||||||||
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Title | How an Epidermal Growth Factor (EGF)-Like Domain Binds Calcium-High Resolution NMR Structure of the Calcium Form of the NH2-Terminal EGF-Like Domain in Coagulation Factor X | ||||||||||||
![]() | COAGULATION FACTOR X | ||||||||||||
![]() | COAGULATION FACTOR | ||||||||||||
Function / homology | ![]() coagulation factor Xa / positive regulation of leukocyte chemotaxis / blood coagulation / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | SOLUTION NMR | ||||||||||||
![]() | Selander-Sunnerhagen, M. / Ullner, M. / Persson, M. / Teleman, O. / Stenflo, J. / Drakenberg, T. | ||||||||||||
![]() | ![]() Title: How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X. Authors: Selander-Sunnerhagen, M. / Ullner, M. / Persson, E. / Teleman, O. / Stenflo, J. / Drakenberg, T. #1: ![]() Title: Three-Dimensional Structure of the Apo Form of the N-Terminal Egf-Like Module of Blood Coagulation Factor X as Determined by NMR Spectroscopy and Simulated Folding Authors: Ullner, M. / Selander, M. / Persson, E. / Stenflo, J. / Teleman, O. / Drakenberg, T. #2: ![]() Title: 1H NMR Assignment and Secondary Structure of the Ca2+-Free Form of the Amino-Terminal Epidermal Growth Factor Like Domain in Coagulation Factor X Authors: Selander, M. / Persson, E. / Stenflo, J. / Drakenberg, T. #3: ![]() Title: Calcium Binding to the Isolated Beta-Hydroxyaspartic Acid-Containing Epidermal Growth Factor-Like Domain of the Bovine Factor X Authors: Selander, M. / Persson, E. / Drakenberg, T. / Linse, S. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 180.3 KB | Display | ![]() |
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PDB format | ![]() | 147.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 360.8 KB | Display | ![]() |
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Full document | ![]() | 466.2 KB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 27.3 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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1 |
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Atom site foot note | 1: THE HYDROXYLATED ASPARTIC ACID RESIDUE IS REPRESENTED AS ASP 63 AND HETATM HYD 63. 2: PHE 83 - SER 84 MODEL 3 OMEGA =216.47 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: SER 84 - THR 85 MODEL 3 OMEGA =148.06 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: PHE 83 - SER 84 MODEL 4 OMEGA =213.40 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: SER 84 - THR 85 MODEL 4 OMEGA =148.79 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: SER 84 - THR 85 MODEL 5 OMEGA =211.34 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: PHE 83 - SER 84 MODEL 9 OMEGA =214.90 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 8: SER 84 - THR 85 MODEL 9 OMEGA =147.72 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4576.948 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR ensemble | Conformers submitted total number: 15 |
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