MolNFT v1 · #68378 · protein

Crystal structure analysis of endosialidasenf at 0.98 a resolution

3JU4 · Endo-N-acetylneuraminidase: “Crystal structure analysis of endosialidasenf at 0.98 a resolution”. X-ray diffraction, 3 ligands (SLB, NA, CL), 4 pockets (best druggability 0.51). MolNFT v1 #68378 on GenesisL1: 3D structure, binding…

PDB: 3JU4
Type: protein
Length: 670 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-N-acetylneuraminidase
EC: 3.2.1.129
UniProt: Q04830
Ligands: SLB, NA, CL
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-N-acetylneuraminidase (EC 3.2.1.129)	protein	670	3% helix, 37% strand	Q04830

Ligands and binding sites

SLB · N-acetyl-beta-neuraminic acid · sugar · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	197	0.51	0.77	18	empty
2	189	0.46	0.76	26	CL
3	135	0.39	0.74	25	empty
4	87	0.39	0.77	20	empty

Compared structures

3JU4 · Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution · 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 Q04830
Elsewhere: RCSB PDB 3JU4 · PDBe 3JU4 · UniProt Q04830

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