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1.8 ångström human fascin 1 crystal structure

Analyse 1.8 ångström human fascin 1 crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LLP
Type: protein
Length: 950 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fascin
UniProt: Q16658
Ligands: K, BR, SO4
Pockets: 10 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fascin	protein	472	7% helix, 49% strand	Q16658
B	Fascin	protein	478	6% helix, 48% strand	Q16658

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, B
BR · Bromide ion · ion · 7 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains B
GOL · Glycerol · additive · 5 copies · chains A, B
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B

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

Pockets

10 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	546	0.74	0.82	45	empty
2	446	0.62	0.76	63	GOL
3	265	0.53	0.76	32	empty
4	92	0.48	0.81	17	empty
5	224	0.48	0.74	36	empty

Interfaces

1 interface between chains.

A–B · 670 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3LLP · 1.8 Angstrom human fascin 1 crystal structure · the same entry in another collection · chain A against A, TM-score 1.00
Q16658 · AlphaFold monomer V2.0 prediction for fascin (Q16658) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q16658
Elsewhere: RCSB PDB 3LLP · PDBe 3LLP · UniProt Q16658

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