MolNFT v1 · #109942 · protein

Bacillus thuringiensis parm with amppnp

4XHN · Uncharacterized protein: “Bacillus thuringiensis parm with amppnp”. X-ray diffraction, 2 ligands (ANP, MG), 3 pockets (best druggability 0.80). MolNFT v1 #109942 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4XHN
Type: protein
Length: 358 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A0A024E1G1
Ligands: ANP, MG
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	358	36% helix, 27% strand	A0A024E1G1

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · 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	1194	0.80	0.81	100	MG, ANP
2	59	0.31	0.76	12	empty
3	60	0.30	0.74	19	empty

Compared structures

4XHN · Bacillus thuringiensis ParM with AMPPNP · 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 4XHN · PDBe 4XHN · UniProt A0A024E1G1

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