Research workbench

Gelsolin G4-G6/ACTIN complex

Analyse Gelsolin G4-G6/ACTIN complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H1V
Type: protein
Length: 695 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin; Gelsolin
UniProt: P02568, P06396
Ligands: ATP, CA
Pockets: 7 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Actin	protein	368	42% helix, 19% strand	P02568
G	Gelsolin	protein	327	19% helix, 28% strand	P06396

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
CA · Calcium ion · metal · 5 copies · chains A, G

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

Pockets

7 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	381	0.74	0.85	53	CA, ATP
2	1065	0.73	0.77	100	empty
3	180	0.67	0.86	34	empty
4	202	0.60	0.82	33	empty
5	66	0.43	0.81	16	empty

Interfaces

1 interface between chains.

A–G · 1113 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1H1V · gelsolin G4-G6/actin complex · the same entry in another collection · chain A against A, TM-score 1.00
P06396 · AlphaFold monomer V2.0 prediction for gelsolin (P06396) · a predicted model of the same protein · chain G against A, TM-score 0.62

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 P02568
Every structure of UniProt P06396
Elsewhere: RCSB PDB 1H1V · PDBe 1H1V · UniProt P02568 · UniProt P06396

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