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Crystal structure of the N-terminal domain of caseinolytic protease associated chaperone CLPC1 from arabidopsis thaliana

Analyse Crystal structure of the N-terminal domain of caseinolytic protease associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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.

Pocket	Volume (Å³)	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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