MolNFT v1 · #91422 · protein

Crystal structure of the C-terminal domain of clpb

4FCT · Chaperone protein clpb: “Crystal structure of the C-terminal domain of clpb”. X-ray diffraction, 2 pockets (best druggability 0.59). MolNFT v1 #91422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4FCT
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein clpb
UniProt: Q9RA63
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein clpb	protein	292	51% helix, 15% strand	Q9RA63

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	325	0.59	0.77	32	empty
2	51	0.28	0.75	14	empty

Compared structures

4FCT · Crystal structure of the C-terminal domain of ClpB · the same entry in another collection · chain A against A, TM-score 1.00
Q9RA63 · AlphaFold monomer V2.0 prediction for chaperone protein clpb (Q9RA63) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 4FCT · PDBe 4FCT · UniProt Q9RA63

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