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- PDB-1cpb: STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION -

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Basic information

Entry
Database: PDB / ID: 1cpb
TitleSTRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION
Components(CARBOXYPEPTIDASE B) x 2
KeywordsHYDROLASE (C-TERMINAL PEPTIDASE)
Function / homology
Function and homology information


Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase B / metallocarboxypeptidase activity / cytoplasmic vesicle / proteolysis / extracellular space / zinc ion binding
Similarity search - Function
Carboxypeptidase B, carboxypeptidase domain / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Zinc carboxypeptidases, zinc-binding region 2 signature. / Zinc carboxypeptidases, zinc-binding region 1 signature. / Zn_pept / Peptidase family M14 domain profile. / Peptidase M14, carboxypeptidase A / Zinc carboxypeptidase
Similarity search - Domain/homology
Biological speciesBos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsSchmid, 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.
History
DepositionJun 23, 1976Processing site: BNL
Revision 1.0Nov 14, 1977Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CARBOXYPEPTIDASE B
B: CARBOXYPEPTIDASE B


Theoretical massNumber of molelcules
Total (without water)33,8612
Polymers33,8612
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.940, 54.940, 104.600
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32

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Components

#1: Protein CARBOXYPEPTIDASE B / Coordinate model: Cα atoms only


Mass: 9353.436 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Organ: PANCREAS / References: UniProt: P00732, carboxypeptidase B
#2: Protein CARBOXYPEPTIDASE B / Coordinate model: Cα atoms only


Mass: 24507.484 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Organ: PANCREAS / References: UniProt: P00732, carboxypeptidase B

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.69 Å3/Da / Density % sol: 54.29 %
Crystal grow
*PLUS
Method: other / Details: Schmid, M.F., (1969) J. Mol. Biol., 40, 353.

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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

RefinementHighest resolution: 2.8 Å
Refinement stepCycle: LAST / Highest resolution: 2.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms299 0 0 0 299
Refinement
*PLUS
Lowest resolution: 10 Å / Rfactor obs: 0.325
Solvent computation
*PLUS
Displacement parameters
*PLUS

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