MolNFT v1 · #98761 · protein

Clpb NBD2 from T. thermophilus in complex with ADP

4LJ5 · Chaperone protein clpb: “Clpb NBD2 from T. thermophilus in complex with ADP”. X-ray diffraction, 1 ligand (ADP), 3 pockets (best druggability 0.61). MolNFT v1 #98761 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4LJ5
Type: protein
Length: 320 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 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein clpb	protein	320	51% helix, 15% 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.61	0.79	30	ADP
2	136	0.43	0.75	27	empty
3	80	0.43	0.79	17	empty

Compared structures

4LJ5 · ClpB NBD2 from T. thermophilus in complex with ADP · 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 0.89

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 4LJ5 · PDBe 4LJ5 · UniProt Q9RA63

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