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- PDB-3cms: ENGINEERING ENZYME SUB-SITE SPECIFICITY: PREPARATION, KINETIC CHA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3cms | ||||||
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Title | ENGINEERING ENZYME SUB-SITE SPECIFICITY: PREPARATION, KINETIC CHARACTERIZATION AND X-RAY ANALYSIS AT 2.0-ANGSTROMS RESOLUTION OF VAL111PHE SITE-MUTATED CALF CHYMOSIN | ||||||
![]() | CHYMOSIN B | ||||||
![]() | HYDROLASE / ACID PROTEINASE | ||||||
Function / homology | ![]() chymosin / digestion / aspartic-type endopeptidase activity / proteolysis Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Newman, M. / Frazao, C. / Shearer, A. / Tickle, I.J. / Blundell, T.L. | ||||||
![]() | ![]() Title: Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin. Authors: Strop, P. / Sedlacek, J. / Stys, J. / Kaderabkova, Z. / Blaha, I. / Pavlickova, L. / Pohl, J. / Fabry, M. / Kostka, V. / Newman, M. #1: ![]() Title: X-Ray Analyses of Aspartic Proteinases Iv: Structure and Refinement at 2.2 Angstroms Resolution of Bovine Chymosin Authors: Newman, M. / Safro, M. / Frazao, C. / Kahn, G. / Zdanov, A. / Tickle, I.J. / Blundell, T.L. / Andreeva, 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 | ![]() | 73.1 KB | Display | ![]() |
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PDB format | ![]() | 56.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369.8 KB | Display | ![]() |
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Full document | ![]() | 388.7 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 15.5 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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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE PRO 23 IS A CIS-PROLINE. 2: THESE RESIDUES ARE IN POORLY DEFINED REGIONS IN THE ELECTRON DENSITY MAP. 3: RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE CONFORMATIONS. THESE RESIDUES ARE IN POORLY DEFINED REGIONS IN THE ELECTRON DENSITY MAP. CONFORMATION B HAS THE HIGHER RELATIVE OCCUPANCY (O.60) ...3: RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE CONFORMATIONS. THESE RESIDUES ARE IN POORLY DEFINED REGIONS IN THE ELECTRON DENSITY MAP. CONFORMATION B HAS THE HIGHER RELATIVE OCCUPANCY (O.60) AND IS ASSOCIATED WITH SUPERIOR ELECTRON DENSITY. THUS IT APPEARS THAT CONFORMATION B IS SIGNIFICANTLY MORE HIGHLY POPULATED THAN CONFORMATION A. CONFORMATION A WITH OCCUPANCY OF 0.40 MUST BE REGARDED AS A TENTATIVE INTERPRETATION. |
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Components
#1: Protein | Mass: 35720.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | THE SPECIFIC GENE MUTATION V111F IS SITUATED BETWEEN THE PRIMARY SPECIFICITY BINDING POCKET S1 AND ...THE SPECIFIC GENE MUTATION V111F IS SITUATED BETWEEN THE PRIMARY SPECIFICIT |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.16 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: microdialysis | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 22098 / % possible obs: 96.4 % / Observed criterion σ(I): 0.072 / Num. measured all: 149939 / Rmerge(I) obs: 3 |
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Processing
Software | Name: RESTRAIN / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å Details: THE QUANTITY PRESENTED IN THE TEMPERATURE FACTOR FIELD IS U. RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE CONFORMATIONS. TURN 5 WITH THE A CONFORMATION IS CLASSIFED TYPE II' 2:2 ...Details: THE QUANTITY PRESENTED IN THE TEMPERATURE FACTOR FIELD IS U. RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE CONFORMATIONS. TURN 5 WITH THE A CONFORMATION IS CLASSIFED TYPE II' 2:2 DISTORTED. TURN 5 WITH THE B CONFORMATION IS UNCLASSIFIED 2:2. INVARIANT RESIDUE TYR 14 HAS BEEN BUILT INTO A CONFORMATION THAT DIFFERS FROM THE WILD-TYPE CHYMOSIN STRUCTURE. HOWEVER, THIS RESIDUE BELONGS TO THE POORLY DEFINED SURFACE REGION BETWEEN STRANDS AN AND BN, AND THUS THE ASSIGNMENT OF ITS POSITION MUST BE REGARDED AS TENTATIVE.
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.195 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 30.3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_plane_restr / Dev ideal: 0.019 |