Research workbench
Crystal structure of clostridium thermocellum RSGI9 S1C-NTF2 bi-domain
Analyse Crystal structure of clostridium thermocellum RSGI9 S1C-NTF2 bi-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SJY
- Type
- protein
- Length
- 625 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-sigma-I factor RSGI9
- UniProt
- A3DC20
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-sigma-I factor RSGI9 | protein | 313 | 21% helix, 42% strand | A3DC20 |
| B | Anti-sigma-I factor RSGI9 | protein | 312 | 21% helix, 42% strand | A3DC20 |
Ligands and binding sites
- GOL · Glycerol · additive · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.67 | 0.79 | 56 | GOL |
| 2 | 343 | 0.58 | 0.76 | 35 | GOL |
| 3 | 189 | 0.53 | 0.78 | 26 | GOL |
| 4 | 165 | 0.53 | 0.79 | 26 | GOL |
| 5 | 80 | 0.42 | 0.79 | 19 | GOL |
Interfaces
1 interface between chains.
- A–B · 957 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 7SJY · Crystal structure of Clostridium thermocellum RsgI9 S1C-NTF2 bi-domain · the same entry in another collection · chain A against A, TM-score 1.00
- A3DC20 · AlphaFold monomer V2.0 prediction for anti-sigma-I factor RSGI9 (A3DC20) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 A3DC20
- Elsewhere: RCSB PDB 7SJY · PDBe 7SJY · UniProt A3DC20
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