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- PDB-1pco: SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pco | ||||||
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Title | SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR | ||||||
![]() | PORCINE PANCREATIC PROCOLIPASE B | ||||||
![]() | LIPASE PROTEIN COFACTOR | ||||||
Function / homology | ![]() Digestion of dietary lipid / Retinoid metabolism and transport / lipase binding / response to food / lipid catabolic process / enzyme activator activity / digestion / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Breg, J.N. / Sarda, L. / Cozzone, P.J. / Rugani, N. / Boelens, R. / Kaptein, R. | ||||||
![]() | ![]() Title: Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR. Authors: Breg, J.N. / Sarda, L. / Cozzone, P.J. / Rugani, N. / Boelens, R. / Kaptein, R. #1: ![]() Title: A Protein Fold Element Comprising a Triple-Strand B-Sheet and Two Disulphide Bridges Recognized in Procolipase and Other Unrelated Proteins Authors: Breg, J.N. / Ujah, E.C. / Sarda, L. / Cozzone, P.J. / Kaptein, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 349.5 KB | Display | ![]() |
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PDB format | ![]() | 293.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.9 KB | Display | ![]() |
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Full document | ![]() | 526.4 KB | Display | |
Data in XML | ![]() | 39.9 KB | Display | |
Data in CIF | ![]() | 67.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: GLY 56 - VAL 57 MODEL 3 OMEGA = 83.78 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: GLY 56 - VAL 57 MODEL 18 OMEGA = 139.93 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLY 56 - VAL 57 MODEL 20 OMEGA = 145.78 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: GLY 56 - VAL 57 MODEL 25 OMEGA = 110.16 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein | Mass: 10117.486 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: 25 |
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