[English] 日本語
![](img/lk-miru.gif)
- PDB-1rac: CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYL... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1rac | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | ||||||
![]() |
| ||||||
![]() | TRANSFERASE | ||||||
Function / homology | ![]() aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kosman, R.P. / Gouaux, J.E. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Authors: Kosman, R.P. / Gouaux, J.E. / Lipscomb, W.N. #1: ![]() Title: Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase: Crystal Structures of the Unligated and ATP-and Ctp-Complexed Enzymes at 2.6 Angstroms Resolution Authors: Stevens, R.C. / Gouaux, J.E. / Lipscomb, W.N. #2: ![]() Title: Structural Asymmetry in the Ctp-Liganded Form of Aspartate Carbamoyltransferase from Escherichia Coli Authors: Kim, K.H. / Pan, Z. / Honzatko, R.B. / Ke, H.-M. / Lipscomb, W.N. #3: ![]() Title: Location of Amino Acid Alterations in Mutants of Aspartate Transcarbamoylase: Structural Aspects of Interallelic Complementation Authors: Schachman, H.K. / Pauza, C.D. / Navre, M. / Karels, M.J. / Wu, L. / Yang, Y.R. #4: ![]() Title: Nucleotide Sequence of the Structural Gene (Pyrb) that Encodes the Catalytic Polypeptide of Aspartate Transcarbamoylase of Escherichia Coli Authors: Hoover, T.A. / Roof, W.D. / Foltermann, K.F. / O'Donovan, G.A. / Bencini, D.A. / Wild, J.R. #5: ![]() Title: Amino Acid Sequence of the Catalytic Subunit of Aspartate Transcarbamoylase from Escherichia Coli Authors: Konigsberg, W.H. / Henderson, L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 193.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 153.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1raaC ![]() 1rabC ![]() 1radC ![]() 1raeC ![]() 1rafC ![]() 1ragC ![]() 1rahC ![]() 1raiC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO A 268 / 2: CIS PROLINE - PRO C 268 |
-
Components
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | THE AMINO ACID SEQUENCE OF ESCHERICHIA COLI ATCASE USED IN THIS ENTRY REPRESENTS A DEPARTURE FROM ...THE AMINO ACID SEQUENCE OF ESCHERICHI | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.71 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 5.8 / Method: microdialysisDetails: taken from Gouaux, J. E. et al (1989). Biochemistry, 28, 1798-1803. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / Num. obs: 35204 / % possible obs: 82 % / Observed criterion σ(I): 2 / Num. measured all: 169691 / Rmerge(I) obs: 0.097 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.189 / Rfactor obs: 0.189 / Highest resolution: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.189 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|