MolNFT v1 · #164601 · protein + RNA
Atomic model for turnip mosaic virus (tumv)
6T34 · Coat protein: “Atomic model for turnip mosaic virus (tumv)”. Electron microscopy, 20 pockets (best druggability 0.89). MolNFT v1 #164601 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6T34
- Type
- protein + RNA
- Length
- 4,028 residues
- Chains
- 38
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coat protein; RNA (5'-R(P*UP*UP*UP*UP*U)-3')
- UniProt
- A0A1B1RVA3
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 2 distinct chains · 36% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S | Coat protein | protein | 207 | 36% helix, 3% strand | A0A1B1RVA3 |
| a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s | RNA (5'-R(P*UP*UP*UP*UP*U)-3') | rna | 5 | — | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1104 | 0.89 | 0.91 | 162 | empty |
| 2 | 975 | 0.89 | 0.91 | 156 | empty |
| 3 | 965 | 0.89 | 0.91 | 154 | empty |
| 4 | 679 | 0.87 | 0.91 | 103 | empty |
| 5 | 698 | 0.87 | 0.91 | 105 | empty |
Interfaces
155 interfaces between chains.
- A–B · 1940 Ų buried · 24 hydrogen bonds · protein-protein
- F–G · 1937 Ų buried · 24 hydrogen bonds · protein-protein
- I–J · 1936 Ų buried · 24 hydrogen bonds · protein-protein
- K–L · 1935 Ų buried · 24 hydrogen bonds · protein-protein
- H–I · 1934 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 isopeptide (isopeptide).
Compared structures
- 6T34 · Atomic model for Turnip mosaic virus (TuMV) · 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 A0A1B1RVA3
- Elsewhere: RCSB PDB 6T34 · PDBe 6T34 · UniProt A0A1B1RVA3
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