Research workbench

Leech intramolecular trans-sialidase complexed with dana

Analyse Leech intramolecular trans-sialidase complexed with dana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SLI
Type: protein
Length: 679 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Intramolecular trans-sialidase
EC: 3.2.1.18
UniProt: Q27701
Ligands: DAN
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Intramolecular trans-sialidase (EC 3.2.1.18)	protein	679	5% helix, 46% strand	Q27701

Ligands and binding sites

DAN · 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.70	0.90	27	empty
2	277	0.59	0.79	36	empty
3	241	0.58	0.79	30	DAN
4	196	0.47	0.75	24	empty
5	137	0.44	0.76	19	empty

Compared structures

1SLI · Leech intramolecular trans-sialidase complexed with dana · the same entry in another collection · chain A against A, TM-score 1.00
Q27701 · AlphaFold monomer V2.0 prediction for anhydrosialidase (Q27701) · a predicted model of the same protein · 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 Q27701
Elsewhere: RCSB PDB 1SLI · PDBe 1SLI · UniProt Q27701

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