MolNFT v1 · #27812 · protein

Crystal structure analysis of sialic acid synthase (NEUB)FROM neisseria meningitidis, bound to MN2+, phosphoenolpyruvate, and N- acetyl mannosaminitol

1XUZ · Polysialic acid capsule biosynthesis protein siac: “Crystal structure analysis of sialic acid synthase (NEUB)FROM neisseria meningitidis, bound to MN2+…”. X-ray diffraction, 3 ligands (MMN, PEP, MN), 1 pocket (best druggability…

PDB: 1XUZ
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polysialic acid capsule biosynthesis protein siac
UniProt: Q57265
Ligands: MMN, PEP, MN
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polysialic acid capsule biosynthesis protein siac	protein	348	40% helix, 20% strand	Q57265

Ligands and binding sites

MMN · 5-deoxy-5-{[(1S)-1-hydroxyethyl]amino}-D-glucitol · ligand · chains A
PEP · Phosphoenolpyruvate · ligand · chains A
MN · Manganese (II) ion · metal · 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	304	0.65	0.80	33	MMN, MN, PEP

Compared structures

1XUZ · Crystal structure analysis of sialic acid synthase (NeuB)from Neisseria meningitidis… · 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 Q57265
Elsewhere: RCSB PDB 1XUZ · PDBe 1XUZ · UniProt Q57265

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