› 1th5

Solution NMR

Solution structure of C-terminal domain of NifU-like protein from Oryza sativa

Released:
DOI: 10.2210/pdb1th5/pdb
PDB entry 1th5 coloured by chain, ensemble of 20 models, front view.
PDB entry 1th5 coloured by chain, ensemble of 20 models, side view.
PDB entry 1th5 coloured by chain, ensemble of 20 models, top view.
Source organism: Oryza sativa
Primary publication:
The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.
Kumeta H, Ogura K, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F
J Biomol NMR 38 161-4 (2007)
PMID: 17431550

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183056 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NifU-like protein 1, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 74 amino acids
Theoretical weight: 8.11 KDa
Source organism: Oryza sativa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q84LK7 (Residues: 154-226; Coverage: 32%)
Gene names: LOC_Os12g07700, NIFU1, Os12g0176200
Sequence domains: NifU-like domain
Structure domains: Fe-S cluster assembly (FSCA)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometr,y simulated annealing, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

NMR of plant proteins.
Kaas et al. (2013)
5 other articles

1 mention without citation

Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26.
Martinez-Hackert et al. (2011)