› 1egs

Solution NMR

NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1egs/pdb
PDB entry 1egs coloured by chain, ensemble of 20 models, front view.
PDB entry 1egs coloured by chain, ensemble of 20 models, side view.
PDB entry 1egs coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Interplay of structure and disorder in cochaperonin mobile loops.
Landry SJ, Taher A, Georgopoulos C, van der Vies SM
Proc Natl Acad Sci U S A 93 11622-7 (1996)
PMID: 8876186

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Co-chaperonin GroES Chain: A
Molecule details ›
Chain: A
Length: 11 amino acids
Theoretical weight: 870 Da
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A6F9 (Residues: 19-27; Coverage: 9%)
Gene names: JW4102, b4142, groES, groS, mopB

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: MOLECULAR DYNAMICS AND SIMULATED ANNEALING
Expression system: Not provided

Quick links

Citations

8 review citations

Chaperone-mediated protein folding.
Fink AL. (1999)
7 more

3 mentions without citation

PEP-FOLD: an online resource for de novo peptide structure prediction.
Maupetit et al. (2009)
2 more