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The crystal structure of human fascin 1 R149A K150A R151A mutant

Analyse The crystal structure of human fascin 1 R149A K150A R151A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GP0
Type: protein
Length: 960 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fascin
UniProt: Q16658
Ligands: CL, BR
Pockets: 9 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fascin	protein	477	6% helix, 49% strand	Q16658
B	Fascin	protein	483	6% helix, 47% strand	Q16658

Ligands and binding sites

CL · Chloride ion · ion · 29 copies · chains A, B
BR · Bromide ion · ion · 7 copies · chains A, B
GOL · Glycerol · additive · 10 copies · chains A, B
DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 3 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

9 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	595	0.72	0.80	52	CL
2	542	0.65	0.76	73	GOL, CL
3	301	0.52	0.74	43	CL, GOL
4	212	0.50	0.76	32	GOL
5	80	0.49	0.82	17	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4GP0 · The crystal structure of human fascin 1 R149A K150A R151A mutant · 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 4GP0 · PDBe 4GP0 · UniProt Q16658

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