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Sialidase BT_1020

Analyse Sialidase BT_1020 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MQS
Type: protein
Length: 1,082 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-L-arabinobiosidase
EC: 3.2.1.187
UniProt: A0A0P0FQG4
Ligands: AHR, NA, CA
Pockets: 12 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-L-arabinobiosidase (EC 3.2.1.187)	protein	1082	23% helix, 28% strand	A0A0P0FQG4

Ligands and binding sites

AHR · alpha-L-arabinofuranose · sugar · chains A
NA · Sodium ion · metal · chains A
CA · Calcium ion · metal · chains A

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	203	0.61	0.82	26	empty
2	179	0.60	0.82	26	empty
3	346	0.58	0.77	44	NA
4	139	0.54	0.81	22	AHR
5	149	0.46	0.77	23	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5MQS · Sialidase BT_1020 · 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 A0A0P0FQG4
Elsewhere: RCSB PDB 5MQS · PDBe 5MQS · UniProt A0A0P0FQG4

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