› 6es7

Solution NMR

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins

Released:
DOI: 10.2210/pdb6es7/pdb
PDB entry 6es7 coloured by chain, ensemble of 20 models, front view.
PDB entry 6es7 coloured by chain, ensemble of 20 models, side view.
PDB entry 6es7 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.
Jemth P, Karlsson E, Vögeli B, Guzovsky B, Andersson E, Hultqvist G, Dogan J, Güntert P, Riek R, Chi CN
Sci Adv 4 eaau4130 (2018)
PMID: 30397651

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187752 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nuclear receptor coactivator 3 Chain: A
Molecule details ›
Chain: A
Length: 44 amino acids
Theoretical weight: 4.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6Q9 (Residues: 1045-1086; Coverage: 3%)
Gene names: AIB1, BHLHE42, NCOA3, RAC3, TRAM1
Sequence domains: Nuclear receptor coactivator
CREB-binding protein Chain: B
Molecule details ›
Chain: B
Length: 50 amino acids
Theoretical weight: 5.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 2061-2109; Coverage: 2%)
Gene names: CBP, CREBBP
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 60%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly.
Gianni et al. (2021)
6 more

5 mentions without citation

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.
Jemth et al. (2018)
4 more