MolNFT v1 · #40267 · protein

Crystal structure of multifunctional sialyltransferase from pasteurella multocida with cmp and alpha-lactose bound

2ILV · Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE: “Crystal structure of multifunctional sialyltransferase from pasteurella multocida with cmp and alpha-lactose…”. X-ray diffraction, 3 ligands (C5P, GLC, GAL), 2 pockets (best druggability…

PDB: 2ILV
Type: protein
Length: 378 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE
EC: 2.4.99.4
UniProt: Q15KI8
Ligands: C5P, GLC, GAL
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE (EC 2.4.99.4)	protein	378	42% helix, 19% strand	Q15KI8

Ligands and binding sites

C5P · Cytidine-5'-monophosphate · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A

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

Pockets

2 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	380	0.69	0.81	45	GAL, C5P
2	75	0.43	0.80	18	empty

Compared structures

2ILV · crystal structure of multifunctional sialyltransferase from Pasteurella multocida with… · 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 Q15KI8
Elsewhere: RCSB PDB 2ILV · PDBe 2ILV · UniProt Q15KI8

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