Research workbench
Competence or damage-inducible protein cina from thermus thermophilus
Analyse Competence or damage-inducible protein cina from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CT9
- Type
- protein
- Length
- 777 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cina-like protein
- UniProt
- Q5SHB0
- Ligands
- AMP, NA, SO4
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cina-like protein | protein | 394 | 39% helix, 27% strand | Q5SHB0 |
| B | Cina-like protein | protein | 383 | 40% helix, 28% strand | Q5SHB0 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.80 | 0.83 | 66 | GOL |
| 2 | 104 | 0.74 | 0.95 | 25 | empty |
| 3 | 210 | 0.58 | 0.80 | 26 | SO4, GOL |
| 4 | 184 | 0.57 | 0.81 | 24 | GOL, SO4 |
| 5 | 217 | 0.48 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 3145 Ų buried · 69 hydrogen bonds · protein-protein
Compared structures
- 4CT9 · Competence or damage-inducible protein CinA from Thermus thermophilus · 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 Q5SHB0
- Elsewhere: RCSB PDB 4CT9 · PDBe 4CT9 · UniProt Q5SHB0
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