MolNFT v1 · #88039 · protein

Crystal structure of E. COLI clpb

4CIU · Chaperone protein clpb: “Crystal structure of E. COLI clpb”. X-ray diffraction, 1 ligand (ADP), 8 pockets (best druggability 0.67). MolNFT v1 #88039 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4CIU
Type: protein
Length: 657 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein clpb
UniProt: P63284
Ligands: ADP
Pockets: 8 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein clpb	protein	657	60% helix, 13% strand	P63284

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	633	0.67	0.76	60	empty
2	267	0.60	0.80	33	ADP
3	184	0.52	0.78	25	ADP
4	179	0.48	0.76	24	empty
5	91	0.47	0.81	16	empty

Modifications

Observed in the structure: 17 modified (engineered).

Compared structures

4CIU · Crystal structure of E. coli ClpB · the same entry in another collection · chain A against A, TM-score 1.00
P63284 · AlphaFold monomer V2.0 prediction for chaperone protein clpb (P63284) · 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 P63284
Elsewhere: RCSB PDB 4CIU · PDBe 4CIU · UniProt P63284

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