MolNFT v1 · #66365 · protein

Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in clostridium difficile toxin a

3HO6: “Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in clostridium difficile…”. X-ray diffraction, 1 ligand (IHP), 7 pockets (best druggability 0.63). MolNFT v1 #66365 on GenesisL1: 3D structure, binding…

PDB: 3HO6
Type: protein
Length: 495 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toxin a
UniProt: P16154
Ligands: IHP
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Toxin a	protein	251	32% helix, 26% strand	P16154
B	Toxin a	protein	244	33% helix, 27% strand	P16154

Ligands and binding sites

IHP · Inositol hexakisphosphate · ligand · 2 copies · chains A, B

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

Pockets

7 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	266	0.63	0.81	33	IHP
2	189	0.62	0.83	30	IHP
3	139	0.59	0.84	20	empty
4	85	0.47	0.82	16	empty
5	88	0.38	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 489 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3HO6 · Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in… · 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 P16154
Elsewhere: RCSB PDB 3HO6 · PDBe 3HO6 · UniProt P16154

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