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- PDB-1apo: THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1apo | ||||||
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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 | ||||||
![]() | EGF-LIKE MODULE OF BLOOD 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 | ||||||
![]() | Ullner, M. / Selander, M. / Persson, E. / Stenflo, J. / Drakenberg, T. / Teleman, O. | ||||||
![]() | ![]() 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. / Drakenberg, T. / Teleman, O. #1: ![]() 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. #2: ![]() Title: Calcium Binding to the Isolated Beta-Hydroxyaspartic Acid-Containing Epidermal Growth Factor-Like Domain of Bovine Factor X Authors: Persson, E. / Selander, M. / Linse, S. / Drakenberg, T. / Ohlin, A.-K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 153.5 KB | Display | ![]() |
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PDB format | ![]() | 132.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.1 KB | Display | ![]() |
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Full document | ![]() | 456.6 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 24.2 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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Atom site foot note | 1: GLU 82 - PHE 83 MODEL 5 OMEGA =211.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: GLU 82 - PHE 83 MODEL 11 OMEGA =210.27 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLU 82 - PHE 83 MODEL 12 OMEGA =210.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4560.949 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-OH / |
-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: 13 |
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