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Bacillus thuringiensis parm hybrid protein with ADP, containing two parm mutants

Analyse Bacillus thuringiensis parm hybrid protein with ADP, containing two parm mutants in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XHP
Type: protein
Length: 723 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Parm hybrid fusion protein
UniProt: A0A024E1G1
Ligands: ADP, MG
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Parm hybrid fusion protein	protein	723	33% helix, 26% strand	A0A024E1G1

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

6 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	1131	0.81	0.82	116	MG, ADP
2	755	0.79	0.83	78	MG, ADP
3	164	0.56	0.81	20	empty
4	155	0.50	0.78	20	empty
5	61	0.40	0.80	15	empty

Compared structures

4XHP · Bacillus thuringiensis ParM hybrid protein with ADP, containing two ParM mutants · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A024E1G1
Elsewhere: RCSB PDB 4XHP · PDBe 4XHP · UniProt A0A024E1G1

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