Research workbench
Crystal structure of escherichia COLI polyphosphate kinase
Analyse Crystal structure of escherichia COLI polyphosphate kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XDO
- Type
- protein
- Length
- 1,374 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyphosphate kinase
- EC
- 2.7.4.1
- UniProt
- P0A7B1
- Pockets
- 14 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Polyphosphate kinase (EC 2.7.4.1) | protein | 687 | 39% helix, 21% strand | P0A7B1 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 986 | 0.81 | 0.83 | 90 | empty |
| 2 | 1000 | 0.81 | 0.82 | 95 | empty |
| 3 | 635 | 0.75 | 0.81 | 53 | empty |
| 4 | 640 | 0.75 | 0.81 | 61 | empty |
| 5 | 540 | 0.73 | 0.81 | 64 | empty |
Interfaces
1 interface between chains.
- A–B · 1720 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
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 P0A7B1
- Elsewhere: RCSB PDB 1XDO · PDBe 1XDO · UniProt P0A7B1
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