Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
CLOCK-BMAL1 transcription complex and DNA (preferred)
PDBe Complex ID:
PDB-CPX-117574 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
Basic helix-loop-helix ARNT-like protein 1
Molecule details ›
Chain: A
Length: 73 amino acids
Theoretical weight: 8.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Helix-loop-helix DNA-binding domain
Structure domains: Helix-loop-helix DNA-binding domain
Length: 73 amino acids
Theoretical weight: 8.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
O00327 (Residues: 66-128; Coverage: 10%)
Sequence domains: Helix-loop-helix DNA-binding domain
Structure domains: Helix-loop-helix DNA-binding domain
Circadian locomoter output cycles protein kaput
Molecule details ›
Chain: B
Length: 71 amino acids
Theoretical weight: 8.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Helix-loop-helix DNA-binding domain
Structure domains: Helix-loop-helix DNA-binding domain
Length: 71 amino acids
Theoretical weight: 8.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: O15516 (Residues: 29-89; Coverage: 7%)
Sequence domains: Helix-loop-helix DNA-binding domain
Structure domains: Helix-loop-helix DNA-binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-17A
Spacegroup:
P3121
Expression system: Escherichia coli BL21
