Research workbench

Structural and biochemical characterization of a novel carbohydrate binding module of endoglucanase CEL5A from eubacterium cellulosolvens.

Analyse Structural and biochemical characterization of a novel carbohydrate binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AFM
Type: protein
Length: 127 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase CEL5A
UniProt: Q3LHN3

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase CEL5A	protein	127	6% helix, 47% strand	Q3LHN3

Ligands and binding sites

ACT · Acetate ion · additive · 4 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4AFM · Structural and biochemical characterization of a novel Carbohydrate Binding Module of… · 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 Q3LHN3
Elsewhere: RCSB PDB 4AFM · PDBe 4AFM · UniProt Q3LHN3

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