› 1o1d

Electron Microscopy
70Å resolution

MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE

Released:
DOI: 10.2210/pdb1o1d/pdb
PDB entry 1o1d coloured by chain, front view.
PDB entry 1o1d coloured by chain, side view.
PDB entry 1o1d coloured by chain, top view.
Source organisms:
Primary publication:
Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle.
Chen LF, Winkler H, Reedy MK, Reedy MC, Taylor KA
J Struct Biol 138 92-104
PMID: 12160705
Related structures: EMD-1001

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero 32-mer (preferred)
PDBe Complex ID:
PDB-CPX-135956 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Myosin heavy chain, skeletal muscle, adult Chains: A, D, G, J, M, P
Molecule details ›
Chains: A, D, G, J, M, P
Length: 840 amino acids
Theoretical weight: 96.63 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P13538 (Residues: 5-844; Coverage: 43%)
Sequence domains:
Myosin regulatory light chain 11 Chains: B, E, H, K, N, Q
Molecule details ›
Chains: B, E, H, K, N, Q
Length: 145 amino acids
Theoretical weight: 16.06 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P02609 (Residues: 21-164; Coverage: 86%)
Gene names: MYL11, MYLPF, RLC
Myosin light chain 3, skeletal muscle isoform Chains: C, F, I, L, O, R
Molecule details ›
Chains: C, F, I, L, O, R
Length: 147 amino acids
Theoretical weight: 16.06 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P02605 (Residues: 4-150; Coverage: 98%)
Actin, alpha skeletal muscle Chains: 0, 1, 2, 3, 4, 5, 7, 8, 9, V, W, X, Y, Z
Molecule details ›
Chains: 0, 1, 2, 3, 4, 5, 7, 8, 9, V, W, X, Y, Z
Length: 375 amino acids
Theoretical weight: 41.86 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MLY 270 x MLY

Experiments and Validation Details

Entry percentile scores
Resolution: 70Å
Relevant EMDB volumes: EMD-1001

Quick links

Citations

10 review citations

Structural studies by electron tomography: from cells to molecules.
Lucić et al. (2005)
9 more

2 mentions without citation

Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future.
Burley et al. (2022)
1 more