MolNFT v1 · #91430 · protein
Crystal structure of the C-terminal domain of clpb
4FD2 · Chaperone protein clpb: “Crystal structure of the C-terminal domain of clpb”. X-ray diffraction, 1 ligand (ADP), 7 pockets (best druggability 0.64). MolNFT v1 #91430 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FD2
- Type
- protein
- Length
- 924 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein clpb
- UniProt
- Q9RA63
- Ligands
- ADP
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Chaperone protein clpb | protein | 308 | 46% helix, 14% strand | Q9RA63 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.64 | 0.78 | 44 | empty |
| 2 | 296 | 0.61 | 0.79 | 31 | ADP |
| 3 | 297 | 0.59 | 0.78 | 30 | ADP |
| 4 | 283 | 0.58 | 0.78 | 30 | ADP |
| 5 | 160 | 0.47 | 0.77 | 26 | empty |
Interfaces
2 interfaces between chains.
- B–D · 668 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 50 Ų buried · 0 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 Q9RA63
- Elsewhere: RCSB PDB 4FD2 · PDBe 4FD2 · UniProt Q9RA63
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