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Trypanosoma cruzi trans-sialidase in complex with munana (michaelis complex)

Analyse Trypanosoma cruzi trans-sialidase in complex with munana (michaelis complex) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S0J
Type: protein
Length: 623 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trans-sialidase
EC: 3.2.1.18
UniProt: Q26966
Ligands: MUS
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trans-sialidase (EC 3.2.1.18)	protein	623	8% helix, 47% strand	Q26966

Ligands and binding sites

MUS · 4-methyl-2-oxo-2H-chromen-7-yl 5-(acetylamino)-3,5-dideoxy-L-erythro-non-2-ulopyranosidonic acid · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	290	0.66	0.82	31	MUS
2	257	0.57	0.77	22	empty
3	59	0.32	0.76	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1S0J · Trypanosoma cruzi trans-sialidase in complex with MuNANA (Michaelis complex) · 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 Q26966
Elsewhere: RCSB PDB 1S0J · PDBe 1S0J · UniProt Q26966

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