Research workbench

The ligand-bound, open structure of CD0873, a substrate binding protein with adhesive properties from clostridium difficile.

Analyse The ligand-bound, open structure of CD0873, a substrate binding protein with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HNJ
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC-type transport system, sugar-family extracellular solute-binding protein
UniProt: Q18A65
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC-type transport system, sugar-family extracellular solute-binding protein	protein	297	41% helix, 23% strand	Q18A65

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 6 copies · chains A
PGE · Triethylene glycol · additive · chains A
PEG · Di(hydroxyethyl)ether · additive · 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	345	0.57	0.76	46	EDO, PGE

Compared structures

6HNJ · The ligand-bound, open structure of CD0873, a substrate binding protein with adhesive… · 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 Q18A65
Elsewhere: RCSB PDB 6HNJ · PDBe 6HNJ · UniProt Q18A65

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.