Research workbench
Solution structure of the H189Q mutant of the enzyme I dimer using residual dipolar couplings and small angle X-ray scattering
Analyse Solution structure of the H189Q mutant of the enzyme I dimer using residual… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L5H
- Type
- protein
- Length
- 1,146 residues
- Chains
- 2
- Method
- solution nmr; solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoenolpyruvate-protein phosphotransferase
- EC
- 2.7.3.9
- UniProt
- P08839
- Pockets
- 12 · best druggability 0.68
Structure
solution nmr; solution scattering · 1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) | protein | 573 | 52% helix, 12% strand | P08839 |
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.68 | 0.81 | 61 | empty |
| 2 | 209 | 0.68 | 0.85 | 37 | empty |
| 3 | 614 | 0.67 | 0.77 | 66 | empty |
| 4 | 383 | 0.59 | 0.76 | 30 | empty |
| 5 | 231 | 0.56 | 0.79 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 1829 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 2L5H · Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar… · the same entry in another collection · chain A against A, TM-score 1.00
- P08839 · AlphaFold monomer V2.0 prediction for phosphoenolpyruvate-protein phosphotransferase… · a predicted model of the same protein · chain A against A, TM-score 0.61
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P08839
- Elsewhere: RCSB PDB 2L5H · PDBe 2L5H · UniProt P08839
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