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Trypanosoma rangeli sialidase in complex with the inhibitor dana

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

PDB: 1MZ6
Type: protein
Length: 620 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sialidase
EC: 3.2.1.18
UniProt: O44049
Ligands: DAN, NAG
Pockets: 3 · best druggability 0.59

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sialidase (EC 3.2.1.18)	protein	620	7% helix, 46% strand	O44049

Ligands and binding sites

DAN · 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · 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	251	0.59	0.79	32	DAN
2	246	0.57	0.78	25	empty
3	62	0.30	0.75	16	empty

Modifications

Observed in the structure: 5 glycan, 1 disulfide (N-glycosylation, disulfide).

Compared structures

1MZ6 · Trypanosoma rangeli sialidase in complex with the inhibitor DANA · 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 1MZ6 · PDBe 1MZ6 · UniProt O44049

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