Research workbench

Crystal structure of the sialyltransferase PM0188 with cmp

Analyse Crystal structure of the sialyltransferase PM0188 with cmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C84
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE
UniProt: Q15KI8
Ligands: C
Pockets: 4 · best druggability 0.68

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	protein	377	41% helix, 19% strand	Q15KI8

Ligands and binding sites

C · Cytidine-5'-monophosphate · ligand · chains A

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

Pockets

4 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	451	0.68	0.80	49	C
2	88	0.47	0.81	20	empty
3	59	0.38	0.79	14	empty
4	51	0.35	0.79	16	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2C84 · Crystal structure of the sialyltransferase PM0188 with cmp · 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 2C84 · PDBe 2C84 · UniProt Q15KI8

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