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Apo form of the catabolite control protein a (ccpa) from bacillus megaterium, with the DNA binding domain

Analyse Apo form of the catabolite control protein a (ccpa) from bacillus megaterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JCG
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-resistance amylase regulator
UniProt: P46828
Ligands: CA
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-resistance amylase regulator	protein	322	43% helix, 16% strand	P46828

Ligands and binding sites

CA · Calcium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	267	0.65	0.82	38	empty

Compared structures

2JCG · Apo form of the catabolite control protein A (ccpA) from bacillus megaterium, with the… · the same entry in another collection · chain A against A, TM-score 1.00
P46828 · AlphaFold monomer V2.0 prediction for catabolite control protein a (P46828) · a predicted model of the same protein · chain A against A, TM-score 0.79

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 P46828
Elsewhere: RCSB PDB 2JCG · PDBe 2JCG · UniProt P46828

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