› 1m9l

Solution NMR

Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dynein Light Chain 1

Released:
DOI: 10.2210/pdb1m9l/pdb
PDB entry 1m9l coloured by chain, ensemble of 15 models, front view.
PDB entry 1m9l coloured by chain, ensemble of 15 models, side view.
PDB entry 1m9l coloured by chain, ensemble of 15 models, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
Relaxation-based structure refinement and backbone molecular dynamics of the dynein motor domain-associated light chain.
Wu H, Blackledge M, Maciejewski MW, Mullen GP, King SM
Biochemistry 42 57-71 (2003)
PMID: 12515539

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dynein axonemal light chain 1 Chain: A
Molecule details ›
Chain: A
Length: 199 amino acids
Theoretical weight: 22.32 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9XHH2 (Residues: 1-198; Coverage: 100%)
Gene names: CHLREDRAFT_186669, LC1
Sequence domains: Leucine Rich repeats (2 copies)
Structure domains: Ribonuclease Inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Design and regulation of the AAA+ microtubule motor dynein.
Sakato et al. (2004)
3 more

8 mentions without citation

Structural atlas of dynein motors at atomic resolution.
Toda et al. (2018)
7 more