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Yorodumi- PDB-2ctb: THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARB... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ctb | ||||||
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Title | THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL LACTATE | ||||||
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: 1.5 Å | ||||||
Authors | Teplyakov, A. / Wilson, K.S. / Orioli, P. / Mangani, S. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1993 Title: High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate. Authors: Teplyakov, A. / Wilson, K.S. / Orioli, P. / Mangani, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ctb.cif.gz | 73 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ctb.ent.gz | 57.6 KB | Display | PDB format |
PDBx/mmJSON format | 2ctb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ctb_validation.pdf.gz | 414.8 KB | Display | wwPDB validaton report |
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Full document | 2ctb_full_validation.pdf.gz | 418.8 KB | Display | |
Data in XML | 2ctb_validation.xml.gz | 15.2 KB | Display | |
Data in CIF | 2ctb_validation.cif.gz | 22 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ct/2ctb ftp://data.pdbj.org/pub/pdb/validation_reports/ct/2ctb | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: PEPTIDE BONDS BETWEEN RESIDUES SER 197 - TYR 198, PRO 205 - TYR 206, AND ARG 272 - ASP 273 ARE IN CIS CONFORMATION. 2: SIDE CHAINS OF ARG 2, SER 134, AND ARG 276 HAVE WEAK ELECTRON DENSITY. THEIR ATOMIC B FACTORS REACHED THE MAXIMUM VALUE (99.99) ALLOWED BY THE REFINEMENT PROGRAM. |
-Components
#1: Protein | Mass: 34517.480 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: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.73 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 19.423-441 1966 | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.54 Å / Lowest resolution: 3.5 Å / Num. obs: 37803 / % possible obs: 88.7 % / Num. measured all: 91192 / Rmerge(I) obs: 0.043 |
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||
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Refinement | Highest resolution: 1.5 Å Details: SIDE CHAINS OF ARG 2, SER 134, AND ARG 276 HAVE WEAK ELECTRON DENSITY. THEIR ATOMIC B FACTORS REACHED THE MAXIMUM VALUE (99.99) ALLOWED BY THE REFINEMENT PROGRAM.
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Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.54 Å / Num. reflection obs: 37638 / Rfactor obs: 0.151 / Lowest resolution: 8 Å | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS
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