Research workbench
The trimeric structure of divalent cation tolerance protein CUTA1 from thermus thermophilus HB8
Analyse The trimeric structure of divalent cation tolerance protein CUTA1 from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V6H
- Type
- protein
- Length
- 309 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Divalent cation tolerance protein CUTA1
- UniProt
- Q7SIA8
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Divalent cation tolerance protein CUTA1 | protein | 103 | 35% helix, 43% strand | Q7SIA8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.77 | 0.98 | 18 | empty |
| 2 | 112 | 0.55 | 0.83 | 17 | empty |
| 3 | 103 | 0.54 | 0.83 | 16 | SO4 |
| 4 | 103 | 0.53 | 0.82 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1201 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1189 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 1181 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1V6H · The Trimeric Structure Of Divalent Cation Tolerance Protein CutA1 From Thermus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q7SIA8 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (Q7SIA8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q7SIA8
- Elsewhere: RCSB PDB 1V6H · PDBe 1V6H · UniProt Q7SIA8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.