MolNFT v1 · #113435 · protein

Native structure of N-acetylneuramininate lyase (sialic acid aldolase) from aliivibrio salmonicida

5AFD · N-acetylneuraminate lyase: “Native structure of N-acetylneuramininate lyase (sialic acid aldolase) from aliivibrio salmonicida”. X-ray diffraction, 1 pocket (best druggability 0.63). MolNFT v1 #113435 on GenesisL1: 3D structure…

PDB: 5AFD
Type: protein
Length: 300 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylneuraminate lyase
EC: 4.1.3.3
UniProt: B6EI04
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylneuraminate lyase (EC 4.1.3.3)	protein	300	50% helix, 13% strand	B6EI04

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A
GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	347	0.63	0.79	45	EDO

Compared structures

5AFD · Native structure of N-acetylneuramininate lyase (sialic acid aldolase) from Aliivibrio… · 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 B6EI04
Elsewhere: RCSB PDB 5AFD · PDBe 5AFD · UniProt B6EI04

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