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Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle

Analyse Molecular models of averaged rigor crossbridges from tomograms of insect flight… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O1F
Type: protein
Length: 9,736 residues
Chains: 26
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Skeletal muscle myosin II; Skeletal muscle myosin II regulatory light chain; Skeletal…
UniProt: P13538, P02609, P02605, P68135
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 4 distinct chains · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, G, J	Skeletal muscle myosin II	protein	840	47% helix, 13% strand	P13538
B, E, H, K	Skeletal muscle myosin II regulatory light chain	protein	145	58% helix, 3% strand	P02609
C, F, I, L	Skeletal muscle myosin II essential light chain	protein	147	56% helix, 5% strand	P02605
0, 1, 2, 3, 4, 5, 6, 7, 8, V, W, X, Y, Z	Skeletal muscle actin	protein	372	42% helix, 20% strand	P68135

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	1103	0.83	0.84	94	empty
2	1043	0.82	0.83	103	empty
3	1091	0.82	0.83	113	empty
4	1054	0.82	0.83	107	empty
5	1079	0.82	0.83	114	empty

Interfaces

46 interfaces between chains.

G–H · 1616 Å² buried · 21 hydrogen bonds · protein-protein
J–K · 1532 Å² buried · 20 hydrogen bonds · protein-protein
G–6 · 1513 Å² buried · 104 hydrogen bonds · protein-protein
D–5 · 1511 Å² buried · 104 hydrogen bonds · protein-protein
J–7 · 1507 Å² buried · 105 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 180 modified, 10 isopeptide (methylation, isopeptide).

Compared structures

1O1F · Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle · the same entry in another collection · chain H against H, TM-score 1.00

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 P13538
Every structure of UniProt P02609
Every structure of UniProt P02605
Every structure of UniProt P68135
Elsewhere: RCSB PDB 1O1F · PDBe 1O1F · UniProt P13538 · UniProt P02609 · UniProt P02605 · UniProt P68135

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