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Trypanosoma rangeli sialidase in complex with sialic acid

Analyse Trypanosoma rangeli sialidase in complex with sialic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1N1Y
Type: protein
Length: 628 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.8
Source: Trypanosoma rangeli
Molecule: Sialidase
EC: 3.2.1.18
UniProt: O44049
Ligands: SIA
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · resolution 2.8 · 1 distinct chain · 7% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sialidase (EC 3.2.1.18)	protein	628	7% helix, 46% strand	O44049

Ligands and binding sites

SIA · N-acetyl-alpha-neuraminic acid · sugar · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	302	0.61	0.79	33	SIA
2	247	0.57	0.78	27	empty
3	206	0.50	0.76	35	empty
4	51	0.25	0.73	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1N1Y · Trypanosoma rangeli sialidase in complex with sialic acid · 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 O44049
Elsewhere: RCSB PDB 1N1Y · PDBe 1N1Y · UniProt O44049

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