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Structure of plasmodium ACTIN1 filament

Analyse Structure of plasmodium ACTIN1 filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TU4
Type: protein
Length: 1,860 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin-1
UniProt: Q8I4X0
Ligands: 9UE, ADP, MG
Pockets: 18 · best druggability 0.77

Structure

electron microscopy · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, F	Actin-1	protein	372	41% helix, 20% strand	Q8I4X0

Ligands and binding sites

9UE · Jasplakinolide · ligand · 5 copies · chains A, D, F, B, C
ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, F
MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, F

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

Pockets

18 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	370	0.77	0.88	51	MG, ADP
2	396	0.77	0.86	57	MG, ADP
3	367	0.76	0.87	53	MG, ADP
4	413	0.76	0.86	53	MG, ADP
5	363	0.76	0.87	52	MG, ADP

Interfaces

7 interfaces between chains.

A–F · 1114 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 1107 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 1097 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 399 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 396 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6TU4 · Structure of Plasmodium Actin1 filament · the same entry in another collection · chain F against F, TM-score 1.00
Q8I4X0 · AlphaFold monomer V2.0 prediction for actin-1 (Q8I4X0) · a predicted model of the same protein · chain D against A, TM-score 0.95

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 Q8I4X0
Elsewhere: RCSB PDB 6TU4 · PDBe 6TU4 · UniProt Q8I4X0

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