MolNFT v1 · #117594 · protein

The unliganded structure of caldicellulosiruptor saccharolyticus GH5

5ECU · Cellulase: “The unliganded structure of caldicellulosiruptor saccharolyticus GH5”. X-ray diffraction, 1 ligand (CA), 2 pockets (best druggability 0.43). MolNFT v1 #117594 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ECU
Type: protein
Length: 350 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase
EC: 3.2.1.4
UniProt: A4XHB2
Ligands: CA
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulase (EC 3.2.1.4)	protein	350	34% helix, 18% strand	A4XHB2

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 25 copies · chains A
GOL · Glycerol · additive · 7 copies · chains A
ACT · Acetate ion · additive · 7 copies · chains A
MLI · Malonate ion · additive · 3 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	108	0.43	0.77	20	EDO, GOL, CA
2	81	0.34	0.75	21	MLI

Compared structures

5ECU · The unliganded structure of Caldicellulosiruptor saccharolyticus GH5 · 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 A4XHB2
Elsewhere: RCSB PDB 5ECU · PDBe 5ECU · UniProt A4XHB2

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