+Open data
-Basic information
Entry | Database: PDB / ID: 1cpb | ||||||
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Title | STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION | ||||||
Components | (CARBOXYPEPTIDASE B) x 2 | ||||||
Keywords | HYDROLASE (C-TERMINAL PEPTIDASE) | ||||||
Function / homology | Function and homology information carboxypeptidase B / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Schmid, M.F. / Herriott, J.R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1976 Title: Structure of carboxypeptidase B at 2-8 A resolution. Authors: Schmid, M.F. / Herriott, J.R. #1: Journal: J.Mol.Biol. / Year: 1974 Title: The Structure of Bovine Carboxypeptidase B,Results at 5.5 Angstrom Resolution Authors: Schmid, M.F. / Herriott, J.R. / Lattman, E.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cpb.cif.gz | 20.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cpb.ent.gz | 9.7 KB | Display | PDB format |
PDBx/mmJSON format | 1cpb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cpb_validation.pdf.gz | 322.5 KB | Display | wwPDB validaton report |
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Full document | 1cpb_full_validation.pdf.gz | 325 KB | Display | |
Data in XML | 1cpb_validation.xml.gz | 1.2 KB | Display | |
Data in CIF | 1cpb_validation.cif.gz | 3.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cp/1cpb ftp://data.pdbj.org/pub/pdb/validation_reports/cp/1cpb | 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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-Components
#1: Protein | Mass: 9353.436 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00732, carboxypeptidase B |
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#2: Protein | Mass: 24507.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00732, carboxypeptidase B |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.29 % |
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Crystal grow | *PLUS Method: other / Details: Schmid, M.F., (1969) J. Mol. Biol., 40, 353. |
-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 9999 Å / Num. obs: 2581 / Observed criterion σ(I): 2 / Num. measured all: 8709 / Rmerge(I) obs: 0.144 |
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-Processing
Refinement | Highest resolution: 2.8 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refinement | *PLUS Lowest resolution: 10 Å / Rfactor obs: 0.325 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |