MolNFT v1 · #24795 · protein
The trimeric structure of divalent cation tolerance protein CUTA1 from thermus thermophilus HB8
1V6H: “The trimeric structure of divalent cation tolerance protein CUTA1 from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.77). MolNFT v1 #24795 on GenesisL1: 3D structure, binding sites and…
- 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
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