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Single cohesin domain from the scaffolding protein cipa of the clostridium thermocellum cellulosome

Analyse Single cohesin domain from the scaffolding protein cipa of the clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AOH
Type: protein
Length: 290 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulosomal-scaffolding protein a
UniProt: Q06851
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulosomal-scaffolding protein a	protein	143	3% helix, 57% strand	Q06851
B	Cellulosomal-scaffolding protein a	protein	147	3% helix, 57% strand	Q06851

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	390	0.61	0.77	45	empty

Interfaces

1 interface between chains.

A–B · 666 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1AOH · Single cohesin domain from the scaffolding protein cipa of the clostridium thermocellum… · the same entry in another collection · chain A against A, TM-score 1.00
Q06851 · AlphaFold monomer V2.0 prediction for cellulosomal-scaffolding protein a (Q06851) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q06851
Elsewhere: RCSB PDB 1AOH · PDBe 1AOH · UniProt Q06851

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