Research workbench

Crystal structure of the endo-1,4-glucanase, RBCEL1, in complex with cellobiose

Analyse Crystal structure of the endo-1,4-glucanase, RBCEL1, in complex with cellobiose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M24
Type: protein
Length: 321 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase
EC: 3.2.1.4
UniProt: C1JI15
Ligands: BGC
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase (EC 3.2.1.4)	protein	321	36% helix, 16% strand	C1JI15

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 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	173	0.45	0.75	36	BGC

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4M24 · Crystal structure of the endo-1,4-glucanase, RBcel1, in complex with cellobiose · 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 C1JI15
Elsewhere: RCSB PDB 4M24 · PDBe 4M24 · UniProt C1JI15

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