MolNFT v1 · #36156 · protein

Crystal structure of multifunctional sialyltransferase from pasteurella multocida

2EX0 · A2,3-sialyltransferase, A2,6-sialyltransferase: “Crystal structure of multifunctional sialyltransferase from pasteurella multocida”. X-ray diffraction, 10 pockets (best druggability 0.56). MolNFT v1 #36156 on GenesisL1: 3D…

PDB: 2EX0
Type: protein
Length: 782 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: A2,3-sialyltransferase, A2,6-sialyltransferase
EC: 2.4.99.4, 2.4.99.6, 2.4.99.9
UniProt: Q15KI8
Pockets: 10 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	A2,3-sialyltransferase, A2,6-sialyltransferase (EC 2.4.99.4, 2.4.99.6, 2.4.99.9)	protein	392	43% helix, 19% strand	Q15KI8
B	A2,3-sialyltransferase, A2,6-sialyltransferase (EC 2.4.99.4, 2.4.99.6, 2.4.99.9)	protein	390	41% helix, 18% strand	Q15KI8

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	303	0.56	0.76	39	empty
2	314	0.55	0.75	44	empty
3	260	0.55	0.77	35	empty
4	96	0.43	0.78	16	empty
5	97	0.43	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 398 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2EX0 · Crystal structure of multifunctional sialyltransferase from Pasteurella Multocida · 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 2EX0 · PDBe 2EX0 · UniProt Q15KI8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.