MolNFT v1 · #98764 · protein
Clpb NBD2 R621Q from T. thermophilus in complex with ADP
4LJ8 · Chaperone protein clpb: “Clpb NBD2 R621Q from T. thermophilus in complex with ADP”. X-ray diffraction, 1 ligand (ADP), 3 pockets (best druggability 0.59). MolNFT v1 #98764 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4LJ8
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein clpb
- UniProt
- Q9RA63
- Ligands
- ADP
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein clpb | protein | 323 | 51% helix, 16% strand | Q9RA63 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.59 | 0.79 | 27 | ADP |
| 2 | 93 | 0.43 | 0.79 | 14 | empty |
| 3 | 113 | 0.41 | 0.76 | 24 | empty |
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 Q9RA63
- Elsewhere: RCSB PDB 4LJ8 · PDBe 4LJ8 · UniProt Q9RA63
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