[English] 日本語
![](img/lk-miru.gif)
- PDB-2j27: The functional role of the conserved active site proline of trios... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2j27 | ||||||
---|---|---|---|---|---|---|---|
Title | The functional role of the conserved active site proline of triosephosphate isomerase. | ||||||
![]() | TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | ||||||
![]() | ISOMERASE / TIM / 2PG / LOOP7 / GLYCOSOME / TIM-BARREL / GLUCONEOGENESIS / LIPID SYNTHESIS / ATOMIC RESOLUTION / GLYCOLYSIS / PENTOSE SHUNT / POINT MUTATION / FATTY ACID BIOSYNTHESIS / 2-PHOSPHO GLYCOLATE / PROTEIN ENGINEERING | ||||||
Function / homology | ![]() glycosome / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / gluconeogenesis / glycolytic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Casteleijn, M.G. / Alahuhta, M. / Groebel, K. / El-Sayed, I. / Augustyns, K. / Lambeir, A.M. / Neubauer, P. / Wierenga, R.K. | ||||||
![]() | ![]() Title: Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase. Authors: Casteleijn, M.G. / Alahuhta, M. / Groebel, K. / El-Sayed, I. / Augustyns, K. / Lambeir, A.M. / Neubauer, P. / Wierenga, R.K. | ||||||
History |
| ||||||
Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" AND "BA" IN EACH CHAIN ON SHEET ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" AND "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 225 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 181 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 457.4 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 41.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2j24C ![]() 5timS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.724, -0.69), Vector: |
-
Components
#1: Protein | Mass: 26839.795 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.09 % |
---|---|
Crystal grow | pH: 9.5 Details: WELL SOLUTION: 0.1 M CHES PH 9.5, 25 % PEG 1500, 200 MM MGSO4 PROTEIN SOLUTION: 11.5 MG/ML PROTEIN, 20 MM TRIS/HCL PH 7, 100 MM NACL, 1 MM DTT, 1 MM EDTA, 1 MM NAN3 AND 10 MM 2PG |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 2, 2005 / Details: RH COATED, ZERODUR |
Radiation | Monochromator: FIXED EXIT DOUBLE CRYSTAL SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9023 Å / Relative weight: 1 |
Reflection | Resolution: 1.15→25 Å / Num. obs: 164758 / % possible obs: 92 % / Observed criterion σ(I): 3 / Redundancy: 6.8 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 25.12 |
Reflection shell | Resolution: 1.15→1.2 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 5.29 / % possible all: 76.3 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 5TIM Resolution: 1.15→25 Å / Num. parameters: 40486 / Num. restraintsaints: 48408 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
| |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 10 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 17876 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.15→25 Å
| |||||||||||||||||||||||||||||||||
Refine LS restraints |
|