MolNFT v1 · #123483 · protein

Structure of the F-actin-tropomyosin complex (reprocessed)

5JLF · Actin, alpha skeletal muscle: “Structure of the F-actin-tropomyosin complex (reprocessed)”. Electron microscopy, 2 ligands (ADP, MG), 20 pockets (best druggability 0.78). MolNFT v1 #123483 on GenesisL1: 3D structure, binding sites…

PDB: 5JLF
Type: protein
Length: 2,105 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin, alpha skeletal muscle; Tropomyosin alpha-1
UniProt: P68135
Ligands: ADP, MG
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 2 distinct chains · 59% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Actin, alpha skeletal muscle	protein	367	44% helix, 18% strand	P68135
F, G	Tropomyosin alpha-1	protein	135	99% helix, 0% strand	—

Ligands and binding sites

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

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	217	0.78	0.92	41	ADP, MG
2	216	0.78	0.92	45	ADP, MG
3	475	0.78	0.85	67	empty
4	210	0.77	0.92	46	ADP, MG
5	214	0.75	0.90	44	ADP, MG

Interfaces

11 interfaces between chains.

F–G · 1812 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 1197 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1194 Å² buried · 10 hydrogen bonds · protein-protein
D–E · 1191 Å² buried · 10 hydrogen bonds · protein-protein
C–E · 513 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (methylation).

Compared structures

5JLF · Structure of the F-actin-tropomyosin complex (Reprocessed) · the same entry in another collection · chain F against F, TM-score 1.00
P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain C 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 P68135
Elsewhere: RCSB PDB 5JLF · PDBe 5JLF · UniProt P68135

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