Research workbench
B. subtilis gpsb N-terminal domain
Analyse B. subtilis gpsb N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UG3
- Type
- protein
- Length
- 230 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell cycle protein gpsb
- UniProt
- P0CI74
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 4 distinct chains · 67% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell cycle protein gpsb | protein | 66 | 62% helix, 9% strand | P0CI74 |
| B | Cell cycle protein gpsb | protein | 60 | 72% helix, 5% strand | P0CI74 |
| C | Cell cycle protein gpsb | protein | 57 | 70% helix, 11% strand | P0CI74 |
| D | Cell cycle protein gpsb | protein | 47 | 64% helix, 6% strand | P0CI74 |
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 | 176 | 0.48 | 0.76 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2290 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 2016 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 87 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 51 Ų buried · 0 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 P0CI74
- Elsewhere: RCSB PDB 4UG3 · PDBe 4UG3 · UniProt P0CI74
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