Research workbench
Structure of small toprim domain protein from bacillus stearothermophilus.
Analyse Structure of small toprim domain protein from bacillus stearothermophilus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FCJ
- Type
- protein
- Length
- 348 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small toprim domain protein
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small toprim domain protein | protein | 114 | 40% helix, 17% strand | — |
| B | Small toprim domain protein | protein | 118 | 45% helix, 16% strand | — |
| C | Small toprim domain protein | protein | 116 | 45% helix, 16% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains C
- GOL · Glycerol · additive · 2 copies · chains B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.34 | 0.73 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–B · 587 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 581 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 11 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2FCJ · Structure of small TOPRIM domain protein from Bacillus stearothermophilus. · 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
- Elsewhere: RCSB PDB 2FCJ · PDBe 2FCJ
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