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Open data
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Basic information
Entry | Database: PDB / ID: 1cg2 | ||||||
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Title | CARBOXYPEPTIDASE G2 | ||||||
![]() | CARBOXYPEPTIDASE G2 | ||||||
![]() | METALLOCARBOXYPEPTIDASE / HYDROLASE | ||||||
Function / homology | ![]() glutamate carboxypeptidase / carboxypeptidase activity / metallopeptidase activity / proteolysis / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rowsell, S. / Pauptit, R.A. / Tucker, A.D. / Melton, R.G. / Blow, D.M. / Brick, P. | ||||||
![]() | ![]() Title: Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Authors: Rowsell, S. / Pauptit, R.A. / Tucker, A.D. / Melton, R.G. / Blow, D.M. / Brick, P. #1: ![]() Title: A New Crystal Form of Carboxypeptidase G2 from Pseudomonas Sp. Strain Rs-16 which is More Amenable to Structure Determination Authors: Tucker, A.D. / Rowsell, S. / Melton, R.G. / Pauptit, R.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 290.6 KB | Display | ![]() |
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PDB format | ![]() | 231.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.7 KB | Display | ![]() |
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Full document | ![]() | 447.5 KB | Display | |
Data in XML | ![]() | 55.2 KB | Display | |
Data in CIF | ![]() | 77 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Details | THERE ARE TWO MOLECULAR DIMERS CONTAINED WITHIN THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE FOUR SUBUNITS PACK TOGETHER WITH APPROXIMATE D2 SYMMETRY. THE SUBUNITS OF ONE MOLECULE HAVE BEEN ASSIGNED CHAIN IDENTIFIERS *A* AND *D*, WHILE THE SUBUNITS OF THE OTHER MOLECULE HAVE BEEN ASSIGNED CHAIN IDENTIFIERS *B* AND *C*. |
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Components
#1: Protein | Mass: 41748.359 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Water | ChemComp-HOH / | Compound details | EACH MONOMER CONSISTS OF TWO SEPARATE DOMAINS: A CATALYTIC DOMAIN CONTAINING RESIDUES 26 - 213, 326 ...EACH MONOMER CONSISTS OF TWO SEPARATE DOMAINS: A CATALYTIC DOMAIN CONTAINING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 58 % | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: HANGING DROPS WERE FORMED BY MIXING 4 MICROLITERS OF PROTEIN SOLUTION AT 16-20 MG/ML WITH 4 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 10-12% PEG 4000, 0.2M TRIS (PH 7.2), 0.2M ZINC ...Details: HANGING DROPS WERE FORMED BY MIXING 4 MICROLITERS OF PROTEIN SOLUTION AT 16-20 MG/ML WITH 4 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 10-12% PEG 4000, 0.2M TRIS (PH 7.2), 0.2M ZINC ACETATE 10% GLYCEROL. CRYSTALS GREW AT 18-20 DEGREES WITHIN A FEW DAYS., vapor diffusion - hanging drop, temperature 291K | ||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 18, 1996 |
Radiation | Monochromator: Y / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 62936 / % possible obs: 93.9 % / Observed criterion σ(I): 0 / Redundancy: 3.57 % / Biso Wilson estimate: 41.2 Å2 / Rmerge(I) obs: 0.069 / Rsym value: 0.069 / Net I/σ(I): 6.41 |
Reflection shell | Resolution: 2.5→2.63 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.168 / Mean I/σ(I) obs: 4 / % possible all: 90.4 |
Reflection | *PLUS Num. measured all: 224872 |
Reflection shell | *PLUS % possible obs: 90.4 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 37.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS / Rms dev Biso : 3 Å2 / Weight position: 100 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.61 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.196 |