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CWP2 from clostridium difficile

Analyse CWP2 from clostridium difficile in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NJL
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell surface protein (putative S-layer protein)
UniProt: C9YQ15
Ligands: SO4
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell surface protein (putative S-layer protein)	protein	290	22% helix, 34% strand	C9YQ15

Ligands and binding sites

SO4 · Sulfate ion · ion · 20 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.36	0.74	15	empty

Compared structures

5NJL · Cwp2 from Clostridium difficile · 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 C9YQ15
Elsewhere: RCSB PDB 5NJL · PDBe 5NJL · UniProt C9YQ15

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