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Crystal structure of a beta-1,4-endoglucanase from aspergillus niger

Analyse Crystal structure of a beta-1,4-endoglucanase from aspergillus niger in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I77
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1, 4-glucanase
UniProt: A0A023UH08
Ligands: NAG, CA
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1, 4-glucanase	protein	302	36% helix, 19% strand	A0A023UH08

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
CA · Calcium ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
PGE · Triethylene glycol · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.42	0.74	31	PGE, PEG

Modifications

Observed in the structure: 1 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

5I77 · Crystal structure of a beta-1,4-endoglucanase from Aspergillus niger · 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 A0A023UH08
Elsewhere: RCSB PDB 5I77 · PDBe 5I77 · UniProt A0A023UH08

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