MolNFT v1 · #40624 · protein

Crystal structure of the sialyltransferase PM0188 with cmp-3FNEUAC

2IY7 · Lpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE: “Crystal structure of the sialyltransferase PM0188 with cmp-3FNEUAC”. X-ray diffraction, 1 ligand (CSF), 5 pockets (best druggability 0.70). MolNFT v1 #40624 on GenesisL1: 3D structure…

PDB: 2IY7
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE
UniProt: Q15KI8
Ligands: CSF
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE	protein	377	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	373	0.70	0.82	37	CSF
2	89	0.48	0.82	19	empty
3	52	0.33	0.78	12	empty
4	69	0.33	0.75	17	empty
5	53	0.29	0.75	15	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2IY7 · crystal structure of the sialyltransferase PM0188 with CMP-3FNeuAc · 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 2IY7 · PDBe 2IY7 · UniProt Q15KI8

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