PDBe 1l3e

Solution NMR

NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.
Proc. Natl. Acad. Sci. U.S.A. 99 5367-72 (2002)
PMID: 11959990

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hypoxia-inducible factor 1-alpha Chain: A
Molecule details ›
Chain: A
Length: 42 amino acids
Theoretical weight: 4.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: NEW Q16665 (Residues: 786-826; Coverage: 5%)
Gene names: BHLHE78, HIF1A, MOP1, PASD8
Sequence domains: HIF-1 alpha C terminal transactivation domain
Histone acetyltransferase p300 Chain: B
Molecule details ›
Chain: B
Length: 101 amino acids
Theoretical weight: 11.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: NEW Q09472 (Residues: 323-423; Coverage: 4%)
Gene names: EP300, P300
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: distance geometry, simulated annealing
Chemical shifts: BMR5306  
Expression system: Escherichia coli BL21