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Crystal structure of a GH48 cellobiohydrolase from caldicellulosiruptor bescii

Analyse Crystal structure of a GH48 cellobiohydrolase from caldicellulosiruptor bescii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L0G
Type: protein
Length: 627 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 48
UniProt: B9MKU7
Ligands: BGC
Pockets: 1 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 48	protein	627	41% helix, 16% strand	B9MKU7

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 6 copies · chains A
BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · 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	1184	0.85	0.86	108	BGC, EDO, BTB

Compared structures

4L0G · Crystal Structure of a GH48 cellobiohydrolase from Caldicellulosiruptor bescii · 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 B9MKU7
Elsewhere: RCSB PDB 4L0G · PDBe 4L0G · UniProt B9MKU7

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