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Yorodumi- PDB-1cbx: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cbx | ||||||
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Title | CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION | ||||||
Components | CARBOXYPEPTIDASE A | ||||||
Keywords | HYDROLASE(C-TERMINAL PEPTIDASE) | ||||||
Function / homology | Function and homology information carboxypeptidase A / leukotriene metabolic process / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Mangani, S. / Carloni, P. / Orioli, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution. Authors: Mangani, S. / Carloni, P. / Orioli, P. #1: Journal: J.Mol.Biol. / Year: 1983 Title: Refined Crystal Structure of Carboxypeptidase a at 1.54 Angstroms Resolution Authors: Rees, D.C. / Lewis, M. / Lipscomb, W.N. | ||||||
History |
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Remark 700 | SHEET THE PRESENT STRUCTURE MAINTAINS ALL SECONDARY STRUCTURES (HELICES, SHEETS AND TURNS) OF THE ...SHEET THE PRESENT STRUCTURE MAINTAINS ALL SECONDARY STRUCTURES (HELICES, SHEETS AND TURNS) OF THE NATIVE CPA STRUCTURE OF PROTEIN DATA BANK ENTRY 5CPA. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cbx.cif.gz | 74.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cbx.ent.gz | 58.6 KB | Display | PDB format |
PDBx/mmJSON format | 1cbx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cbx_validation.pdf.gz | 391.2 KB | Display | wwPDB validaton report |
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Full document | 1cbx_full_validation.pdf.gz | 412.4 KB | Display | |
Data in XML | 1cbx_validation.xml.gz | 11 KB | Display | |
Data in CIF | 1cbx_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cb/1cbx ftp://data.pdbj.org/pub/pdb/validation_reports/cb/1cbx | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: SER 197 - TYR 198 OMEGA =342.52 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: TYR 198 - SER 199 OMEGA =145.05 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: PRO 205 - TYR 206 OMEGA = 11.68 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: ARG 272 - ASP 273 OMEGA =357.86 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-Components
#1: Protein | Mass: 34442.461 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00730, carboxypeptidase A |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-BZS / |
#4: Water | ChemComp-HOH / |
Sequence details | THE SEQUENCE HAS BEEN TAKEN FROM PROTEIN DATA BANK ENTRY 5CPA. SEQUENCE ADVISORY NOTICE: DIFFERENCE ...THE SEQUENCE HAS BEEN TAKEN FROM PROTEIN DATA BANK ENTRY 5CPA. SEQUENCE ADVISORY NOTICE: DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.85 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: microdialysis | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 22981 / Rmerge(I) obs: 0.055 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.166 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. reflection obs: 15835 / σ(I): 2 / Rfactor obs: 0.166 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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