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- PDB-8cpa: COMPARISON OF THE STRUCTURES OF THREE CARBOXYPEPTIDASE A-PHOSPHON... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8cpa | ||||||
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Title | COMPARISON OF THE STRUCTURES OF THREE CARBOXYPEPTIDASE A-PHOSPHONATE COMPLEXES DETERMINED BY X-RAY CRYSTALLOGRAPHY | ||||||
![]() | CARBOXYPEPTIDASE A | ||||||
![]() | HYDROLASE(C-TERMINAL PEPTIDASE) | ||||||
Function / homology | ![]() carboxypeptidase A / leukotriene metabolic process / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kim, H. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography. Authors: Kim, H. / Lipscomb, W.N. #1: ![]() Title: Synthesis and Evaluation of an Inhibitor of Carboxypeptidase a with a KI Value in the Femtomolar Range Authors: Kaplan, A.P. / Bartlett, P.A. #2: ![]() Title: Crystal Structure of the Complex of Carboxypeptidase a with a Strongly Bound Phosphonate in a New Crystalline Form: Comparison with Structures of Other Complexes Authors: Kim, H. / Lipscomb, W.N. #3: ![]() 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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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.8 KB | Display | ![]() |
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PDB format | ![]() | 59.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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 ANGLE = 1.464 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: ARG 272 - ASP 273 OMEGA ANGLE = 357.278 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: RESIDUE PRO 205 IS A CIS PROLINE. |
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Components
#1: Protein | Mass: 34442.461 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-AGF / |
#4: Water | ChemComp-HOH / |
Sequence details | SEQUENCE ADVISORY NOTICE: THE SEQUENCE WAS OBTAINED FROM REFERENCE 4. DIFFERENCE BETWEEN SWISS-PROT ...SEQUENCE ADVISORY NOTICE: THE SEQUENCE WAS OBTAINED FROM REFERENCE 4. DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.47 % | |||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: referred to 'Kim, H.', (1990) Biochemistry, 29, 5546-5555 | |||||||||||||||
Components of the solutions | *PLUS
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Processing
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Refinement | Rfactor Rwork: 0.186 / Rfactor obs: 0.186 / 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Rfactor obs: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.9 |