Research workbench

Crystal structure of multifunctional sialyltransferase from pasteurella multocida with cmp-3F(EQUATORIAL)-NEU5AC bound

Analyse Crystal structure of multifunctional sialyltransferase from pasteurella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IHK
Type: protein
Length: 376 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: CSF
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 41% 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	376	41% helix, 19% strand	Q15KI8

Ligands and binding sites

CSF · Cytidine-5'-monophosphate-3-fluoro-N-acetyl-neuraminic acid · ligand · chains A

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

Pockets

5 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	404	0.69	0.81	45	CSF
2	77	0.46	0.82	19	empty
3	66	0.38	0.78	14	empty
4	56	0.31	0.76	12	empty
5	50	0.28	0.75	17	empty

Compared structures

2IHK · 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 2IHK · PDBe 2IHK · UniProt Q15KI8

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