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Crystal structure of neunac oxime complexed with neub, an N- acetylneuraminate synthase from neisseria meningitidis

Analyse Crystal structure of neunac oxime complexed with neub, an N- acetylneuraminate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PPY
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylneuraminate synthase
EC: 2.5.1.56
UniProt: H2VFG5
Ligands: OVY
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylneuraminate synthase (EC 2.5.1.56)	protein	348	39% helix, 20% strand	H2VFG5

Ligands and binding sites

OVY · (2E,4S,5R,6R,7S,8R)-5-(acetylamino)-4,6,7,8,9-pentahydroxy-2-(hydroxyimino)nonanoic acid (non-preferred name) · ligand · 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	301	0.64	0.80	34	OVY

Compared structures

6PPY · Crystal structure of NeuNAc oxime complexed with NeuB, an N-acetylneuraminate synthase… · 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 H2VFG5
Elsewhere: RCSB PDB 6PPY · PDBe 6PPY · UniProt H2VFG5

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