› 2l83

Solution NMR

A protein from Haloferax volcanii

Released:
DOI: 10.2210/pdb2l83/pdb
PDB entry 2l83 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l83 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l83 coloured by chain, ensemble of 20 models, top view.
Source organism: Haloferax volcanii DS2
Primary publication:
Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.
Ye K, Liao S, Zhang W, Fan K, Zhang X, Zhang J, Xu C, Tu X
Protein Sci 22 1174-82 (2013)
PMID: 23818097

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small archaeal modifier protein 1 Chain: A
Molecule details ›
Chain: A
Length: 95 amino acids
Theoretical weight: 10.01 KDa
Source organism: Haloferax volcanii DS2
Expression system: Escherichia coli
UniProt:
  • Canonical: D4GUF6 (Residues: 1-87; Coverage: 100%)
Gene names: HVO_2619, samp1
Sequence domains: ThiS family
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 63%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Prokaryotic ubiquitin-like protein modification.
Maupin-Furlow JA. (2014)
4 other articles

1 mention without citation

Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.
Ye et al. (2013)