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Yorodumi- PDB-1apo: THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF... -
+Open data
-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 | ||||||
Components | EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X | ||||||
Keywords | COAGULATION FACTOR | ||||||
Function / homology | Function and homology information coagulation factor Xa / blood coagulation / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Ullner, M. / Selander, M. / Persson, E. / Stenflo, J. / Drakenberg, T. / Teleman, O. | ||||||
Citation | Journal: Biochemistry / Year: 1992 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: Journal: Biochemistry / Year: 1990 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: Journal: J.Biol.Chem. / Year: 1989 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1apo.cif.gz | 153.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1apo.ent.gz | 132.2 KB | Display | PDB format |
PDBx/mmJSON format | 1apo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ap/1apo ftp://data.pdbj.org/pub/pdb/validation_reports/ap/1apo | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Bos taurus (cattle) / References: UniProt: P00743 |
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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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