MolNFT v1 · #182044 · protein

Structure of the autoinhibited state of smooth muscle myosin-2

7MF3 · Myosin-11: “Structure of the autoinhibited state of smooth muscle myosin-2”. Electron microscopy, 3 ligands (ADP, MG, PO4), 20 pockets (best druggability 0.90). MolNFT v1 #182044 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 7MF3
Type: protein
Length: 2,822 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myosin-11; Myosin light polypeptide 6; Myosin regulatory light chain 2, smooth muscle…
UniProt: P10587, P02607, P02612
Ligands: ADP, MG, PO4
Pockets: 20 · best druggability 0.90

Structure

electron microscopy · 7 distinct chains · 58% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myosin-11	protein	890	53% helix, 10% strand	P10587
B	Myosin-11	protein	896	50% helix, 9% strand	P10587
C, F	Myosin light polypeptide 6	protein	149	49% helix, 0% strand	P02607
D	Myosin regulatory light chain 2, smooth muscle major isoform	protein	158	48% helix, 0% strand	P02612
E	Myosin regulatory light chain 2, smooth muscle major isoform	protein	157	54% helix, 3% strand	P02612
G	Myosin-11	protein	212	96% helix, 0% strand	P10587
H	Myosin-11	protein	211	92% helix, 0% strand	P10587

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B, D, E
PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1182	0.90	0.91	146	MG
2	779	0.88	0.91	111	PO4, MG
3	853	0.87	0.89	113	empty
4	1082	0.85	0.85	94	empty
5	485	0.82	0.88	65	empty

Interfaces

14 interfaces between chains.

G–H · 4178 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 3319 Å² buried · 29 hydrogen bonds · protein-protein
A–D · 1740 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1705 Å² buried · 14 hydrogen bonds · protein-protein
B–E · 1416 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7MF3 · Structure of the autoinhibited state of smooth muscle myosin-2 · the same entry in another collection · chain H against H, TM-score 1.00
P10587 · AlphaFold monomer V2.0 prediction for myosin-11 (P10587) · a predicted model of the same protein · chain A against A, TM-score 0.94
P02607 · AlphaFold monomer V2.0 prediction for myosin light polypeptide 6 (P02607) · a predicted model of the same protein · chain C against A, TM-score 0.83

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 P10587
Every structure of UniProt P02607
Every structure of UniProt P02612
Elsewhere: RCSB PDB 7MF3 · PDBe 7MF3 · UniProt P10587 · UniProt P02607 · UniProt P02612

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.