Research workbench
Structure R271L mutant of E. coli pyruvate kinase
Analyse Structure R271L mutant of E. coli pyruvate kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E0U
- Type
- protein
- Length
- 1,844 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Escherichia coli
- Molecule
- Pyruvate kinase
- EC
- 2.7.1.40
- UniProt
- A0A0A0G552
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.8 · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Pyruvate kinase (EC 2.7.1.40) | protein | 461 | 38% helix, 24% strand | A0A0A0G552 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.74 | 0.95 | 26 | empty |
| 2 | 98 | 0.74 | 0.96 | 25 | empty |
| 3 | 748 | 0.71 | 0.77 | 88 | empty |
| 4 | 651 | 0.69 | 0.77 | 72 | empty |
| 5 | 607 | 0.68 | 0.77 | 67 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1122 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1114 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 892 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 884 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1E0U · Structure R271L mutant of E. COLI pyruvate kinase · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0A0G552
- Elsewhere: RCSB PDB 1E0U · PDBe 1E0U · UniProt A0A0A0G552
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