[English] 日本語
![](img/lk-miru.gif)
- PDB-1za1: Structure of wild-type E. coli Aspartate Transcarbamoylase in the... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1za1 | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution | ||||||
![]() |
| ||||||
![]() | TRANSFERASE / ordered substrate binding / cooperativity | ||||||
Function / homology | ![]() aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid metabolic process / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid metabolic process / 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 / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wang, J. / Stieglitz, K.A. / Cardia, J.P. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Authors: Wang, J. / Stieglitz, K.A. / Cardia, J.P. / Kantrowitz, E.R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 205.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 163.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 47.4 KB | Display | |
Data in CIF | ![]() | 67.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1za2C ![]() 1nbeS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00479, UniProt: P0A786*PLUS, aspartate carbamoyltransferase #2: Protein | Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00478, UniProt: P0A7F3*PLUS, aspartate carbamoyltransferase #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.11 % |
---|---|
Crystal grow | Temperature: 293 K / Method: microdialysis / pH: 5.7 Details: 40 mM Citric acid, 3 mM sodium azide, 1mM 2-mercaptoethanol, 1mM CTP, 0.2mM EDTA, pH 5.7, MICRODIALYSIS, temperature 293K |
-Data collection
Diffraction | Mean temperature: 93 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 31, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 80778 / Num. obs: 80374 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.35 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 14.7 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 5.23 % / Rmerge(I) obs: 0.444 / Mean I/σ(I) obs: 3.8 / % possible all: 99 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1NBE Resolution: 2.2→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→30 Å
|