MolNFT v1 · #1820 · protein
Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain
1BDF: “Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain”. X-ray diffraction, 9 pockets (best druggability 0.79). MolNFT v1 #1820 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1BDF
- Type
- protein
- Length
- 917 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase alpha subunit
- EC
- 2.7.7.6
- UniProt
- P0A7Z4
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase alpha subunit (EC 2.7.7.6) | protein | 226 | 21% helix, 36% strand | P0A7Z4 |
| B | RNA polymerase alpha subunit (EC 2.7.7.6) | protein | 232 | 20% helix, 38% strand | P0A7Z4 |
| C | RNA polymerase alpha subunit (EC 2.7.7.6) | protein | 228 | 19% helix, 34% strand | P0A7Z4 |
| D | RNA polymerase alpha subunit (EC 2.7.7.6) | protein | 231 | 19% helix, 35% strand | P0A7Z4 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.79 | 0.82 | 110 | empty |
| 2 | 66 | 0.68 | 0.95 | 17 | empty |
| 3 | 337 | 0.54 | 0.74 | 26 | empty |
| 4 | 288 | 0.52 | 0.74 | 32 | empty |
| 5 | 144 | 0.48 | 0.78 | 21 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1856 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1814 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1038 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 102 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 68 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1BDF · Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain · 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 P0A7Z4
- Elsewhere: RCSB PDB 1BDF · PDBe 1BDF · UniProt P0A7Z4
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