MolNFT v1 · #30521 · protein
Crystal structure of uridylate kinase
2A1F: “Crystal structure of uridylate kinase”. X-ray diffraction, 20 pockets (best druggability 0.83). MolNFT v1 #30521 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2A1F
- Type
- protein
- Length
- 1,406 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridylate kinase
- EC
- 2.7.4.-
- UniProt
- P43890
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 5 distinct chains · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uridylate kinase (EC 2.7.4.-) | protein | 232 | 39% helix, 18% strand | P43890 |
| C | Uridylate kinase (EC 2.7.4.-) | protein | 237 | 38% helix, 19% strand | P43890 |
| D | Uridylate kinase (EC 2.7.4.-) | protein | 236 | 39% helix, 19% strand | P43890 |
| E | Uridylate kinase (EC 2.7.4.-) | protein | 235 | 40% helix, 19% strand | P43890 |
| F | Uridylate kinase (EC 2.7.4.-) | protein | 234 | 39% helix, 19% strand | P43890 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.83 | 0.95 | 40 | empty |
| 2 | 234 | 0.82 | 0.95 | 40 | empty |
| 3 | 238 | 0.82 | 0.94 | 40 | empty |
| 4 | 994 | 0.81 | 0.82 | 66 | empty |
| 5 | 880 | 0.80 | 0.82 | 49 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1409 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 1369 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 1357 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 895 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 874 Ų buried · 4 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 P43890
- Elsewhere: RCSB PDB 2A1F · PDBe 2A1F · UniProt P43890
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