MolNFT v1 · #19712 · protein
RBL2P, beta-tubulin binding post-chaperonin cofactor
1QSD · Protein (beta-tubulin binding post-chaperonin cofactor): “RBL2P, beta-tubulin binding post-chaperonin cofactor”. X-ray diffraction, 3 pockets (best druggability 0.56). MolNFT v1 #19712 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1QSD
- Type
- protein
- Length
- 204 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (beta-tubulin binding post-chaperonin cofactor)
- UniProt
- P48606
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (beta-tubulin binding post-chaperonin cofactor) | protein | 102 | 85% helix, 0% strand | P48606 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.56 | 0.81 | 23 | empty |
| 2 | 71 | 0.54 | 0.86 | 22 | empty |
| 3 | 88 | 0.53 | 0.84 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1229 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 P48606
- Elsewhere: RCSB PDB 1QSD · PDBe 1QSD · UniProt P48606
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