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Structure of tailspike-protein

Analyse Structure of tailspike-protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TYW
Type: protein
Length: 543 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tailspike protein
UniProt: P12528
Ligands: TYV, RAM, MAN, GLA, GLC
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tailspike protein	protein	543	9% helix, 43% strand	P12528

Ligands and binding sites

TYV · alpha-D-Tyvelopyranose · ligand · 2 copies · chains A
RAM · alpha-L-rhamnopyranose · sugar · 2 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
GLA · alpha-D-galactopyranose · sugar · 2 copies · chains A
GLC · alpha-D-glucopyranose · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.45	0.75	27	RAM
2	98	0.37	0.76	21	TYV, GLC
3	94	0.32	0.72	18	empty
4	68	0.30	0.75	13	empty

Compared structures

1TYW · Structure of tailspike-protein · 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 P12528
Elsewhere: RCSB PDB 1TYW · PDBe 1TYW · UniProt P12528

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