MolNFT v1 · #52024 · protein + RNA
Crystal structure of N-terminal domains of human la protein complexed with RNA oligomer uuuuuuuu
2VOO · Lupus la protein: “Crystal structure of N-terminal domains of human la protein complexed with RNA oligomer uuuuuuuu”. X-ray diffraction, 4 pockets (best druggability 0.63). MolNFT v1 #52024 on GenesisL1: 3D structure, binding sites…
- PDB
- 2VOO
- Type
- protein + RNA
- Length
- 362 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lupus la protein; 5'-R(*UP*UP*UP*UP*UP*UP*UP)-3'
- UniProt
- P05455
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lupus la protein | protein | 179 | 40% helix, 22% strand | P05455 |
| B | Lupus la protein | protein | 177 | 41% helix, 22% strand | P05455 |
| C, D | 5'-R(*UP*UP*UP*UP*UP*UP*UP)-3' | rna | 3 | — | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 541 | 0.63 | 0.75 | 58 | empty |
| 2 | 407 | 0.60 | 0.76 | 46 | empty |
| 3 | 110 | 0.39 | 0.76 | 20 | empty |
| 4 | 50 | 0.26 | 0.73 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–D · 464 Ų buried · 10 hydrogen bonds · protein-nucleic
- A–C · 433 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–B · 287 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2VOO · Crystal structure of N-terminal domains of Human La protein complexed with RNA oligomer… · the same entry in another collection · chain A against A, TM-score 1.00
- P05455 · AlphaFold monomer V2.0 prediction for lupus la protein (P05455) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P05455
- Elsewhere: RCSB PDB 2VOO · PDBe 2VOO · UniProt P05455
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