MolNFT v1 · #85424 · protein

The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase family 18, at 1.3A resolution

4AC1 · Endo-N-acetyl-beta-D-glucosaminidase: “The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase family 18, at 1.3A…”. X-ray diffraction, 2 ligands (NAG, ZN), 1 pocket (best druggability 0.36). MolNFT v1…

PDB: 4AC1
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-N-acetyl-beta-D-glucosaminidase
EC: 3.2.1.96
UniProt: C4RA89
Ligands: NAG, ZN
Pockets: 1 · best druggability 0.36

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Endo-N-acetyl-beta-D-glucosaminidase (EC 3.2.1.96)	protein	283	36% helix, 19% strand	C4RA89

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains X
ZN · Zinc ion · metal · 8 copies · chains X
ACT · Acetate ion · additive · 3 copies · chains X

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	94	0.36	0.75	30	ACT, ZN

Modifications

Observed in the structure: 2 glycan (N-glycosylation).

Compared structures

4AC1 · The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase… · the same entry in another collection · chain X against X, 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 C4RA89
Elsewhere: RCSB PDB 4AC1 · PDBe 4AC1 · UniProt C4RA89

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