[English] 日本語
![](img/lk-miru.gif)
- PDB-1asf: THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F)... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1asf | ||||||
---|---|---|---|---|---|---|---|
Title | THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | AMINOTRANSFERASE | ||||||
Function / homology | ![]() L-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase activity / aspartate catabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / protein homodimerization activity / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schumacher, C. / Ringe, D. | ||||||
![]() | ![]() Title: The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase Authors: Schumacher, C. / Ringe, D. #1: ![]() Title: Activity and Structure of the Active Site Mutants R386Y and R386F of Escherichia Coli Aspartate Aminotransferase Authors: Danishefsky, A.T. / Onnufer, J.J. / Petsko, G.A. / Ringe, D. #2: ![]() Title: 2.8 Angstroms Resolution Crystal Structure of an Active Site Mutant of Aspartate Aminotransferase from Escherichia Coli Authors: Smith, D.L. / Almo, S.C. / Toney, M.D. / Ringe, D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 79.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 57.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 396.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 415.3 KB | Display | |
Data in XML | ![]() | 11.4 KB | Display | |
Data in CIF | ![]() | 16.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: ALA 20 - PRO 21 OMEGA =301.68 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: ASP 23 - PRO 24 OMEGA =219.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: ARG 37 - PRO 38 OMEGA = 34.79 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: CIS PROLINE - PRO 140 / 5: CIS PROLINE - PRO 196 6: ASP 200 - PRO 201 OMEGA =147.72 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, 87.3-Y, 80.19-Z) TO THE COORDINATES IN THIS ENTRY. |
-
Components
#1: Protein | Mass: 43603.211 Da / Num. of mol.: 1 / Mutation: Y214F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-PLP / |
Nonpolymer details | HET GROUP PLP 258 IS BOUND TO LYS 258 FORMING A PROTONATED SCHIFF BASE LINKAGE (BETWEEN NZ LYS 258 ...HET GROUP PLP 258 IS BOUND TO LYS 258 FORMING A PROTONATED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.9 % |
---|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.22 / Rfactor obs: 0.22 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|