MolNFT v1 · #53189 · protein

Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin cdta from clostridium difficile

2WN6 · ADP-ribosyltransferase enzymatic component: “Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin cdta…”. X-ray diffraction, 1 ligand (NDP), 4 pockets (best druggability 0.60). MolNFT…

PDB: 2WN6
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosyltransferase enzymatic component
UniProt: Q9KH42
Ligands: NDP
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosyltransferase enzymatic component	protein	404	39% helix, 29% strand	Q9KH42

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
GOL · Glycerol · additive · chains A

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

Pockets

4 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	403	0.60	0.76	49	GOL
2	263	0.56	0.77	37	NDP
3	286	0.52	0.75	28	empty
4	59	0.28	0.73	12	empty

Compared structures

2WN6 · Structural Basis for Substrate Recognition in the Enzymatic Component of… · 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 Q9KH42
Elsewhere: RCSB PDB 2WN6 · PDBe 2WN6 · UniProt Q9KH42

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