MolNFT v1 · #120263 · protein
Crystal structure of the N-terminal domain of caseinolytic protease associated chaperone CLPC1 from arabidopsis thaliana
5GUI · Chaperone protein CLPC1, chloroplastic: “Crystal structure of the N-terminal domain of caseinolytic protease associated chaperone CLPC1 from…”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.33). MolNFT v1 #120263…
- PDB
- 5GUI
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein CLPC1, chloroplastic
- UniProt
- Q9FI56
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CLPC1, chloroplastic | protein | 148 | 64% helix, 3% strand | Q9FI56 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.33 | 0.78 | 10 | empty |
Compared structures
- 5GUI · Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FI56 · AlphaFold monomer V2.0 prediction for chaperone protein CLPC1, chloroplastic (Q9FI56) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9FI56
- Elsewhere: RCSB PDB 5GUI · PDBe 5GUI · UniProt Q9FI56
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