Research workbench

T-plastin-F-actin complex, anti-parallel bundled state

Analyse T-plastin-F-actin complex, anti-parallel bundled state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SX9
Type: protein
Length: 2,668 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin, alpha skeletal muscle; Plastin-3
UniProt: P68139, P13797
Ligands: ADP, MG
Pockets: 20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 51% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, G, E, H	Actin, alpha skeletal muscle	protein	370	45% helix, 20% strand	P68139
D	Plastin-3	protein	448	56% helix, 0% strand	P13797

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains B, A, C, G, E, H
MG · Magnesium ion · metal · 6 copies · chains B, A, C, G, E, H

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

Pockets

20 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	1149	0.80	0.81	86	empty
2	284	0.76	0.89	49	ADP, MG
3	293	0.76	0.88	52	ADP, MG
4	301	0.76	0.88	51	ADP, MG
5	302	0.75	0.88	53	ADP, MG

Interfaces

10 interfaces between chains.

A–D · 1267 Å² buried · 33 hydrogen bonds · protein-protein
E–H · 1169 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1158 Å² buried · 13 hydrogen bonds · protein-protein
E–D · 915 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 604 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (methylation).

Compared structures

7SX9 · T-Plastin-F-actin complex, anti-parallel bundled state · the same entry in another collection · chain D against D, TM-score 1.00
P68139 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68139) · a predicted model of the same protein · chain E against A, TM-score 0.96

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 P68139
Every structure of UniProt P13797
Elsewhere: RCSB PDB 7SX9 · PDBe 7SX9 · UniProt P68139 · UniProt P13797

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