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Open data
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Basic information
Entry | Database: PDB / ID: 1aye | ||||||
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Title | HUMAN PROCARBOXYPEPTIDASE A2 | ||||||
![]() | PROCARBOXYPEPTIDASE A2 | ||||||
![]() | SERINE PROTEASE / ZYMOGEN / HYDROLASE | ||||||
Function / homology | ![]() carboxypeptidase A2 / protein catabolic process in the vacuole / vacuole / metallocarboxypeptidase activity / carboxypeptidase activity / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Garcia-Saez, I. / Reverte, D. / Vendrell, J. / Aviles, F.X. / Coll, M. | ||||||
![]() | ![]() Title: The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. Authors: Garcia-Saez, I. / Reverter, D. / Vendrell, J. / Aviles, F.X. / Coll, M. #1: ![]() Title: Three-Dimensional Structure of Porcine Pancreatic Procarboxypeptidase A. A Comparison of the a and B Zymogens and Their Determinants for Inhibition and Activation Authors: Guasch, A. / Coll, M. / Aviles, F.X. / Huber, R. #2: ![]() Title: Three-Dimensional Structure of Porcine Procarboxypeptidase B: A Structural Basis of its Inactivity Authors: Coll, M. / Guasch, A. / Aviles, F.X. / Huber, 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 | ![]() | 92 KB | Display | ![]() |
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PDB format | ![]() | 71.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.4 KB | Display | ![]() |
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Full document | ![]() | 423.1 KB | Display | |
Data in XML | ![]() | 17.5 KB | Display | |
Data in CIF | ![]() | 24.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1pcaS S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 45006.656 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
Compound details | ZYMOGEN OF ZINC-CONTAINING |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 48.24 % | ||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1997 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. obs: 38772 / % possible obs: 94 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.047 / Net I/σ(I): 32.6 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.178 / Mean I/σ(I) obs: 9.1 / % possible all: 87.9 |
Reflection shell | *PLUS % possible obs: 87.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1PCA Resolution: 1.8→8 Å / Cross valid method: FREE R-FACTOR / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |