Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Chromodomain-helicase-DNA-binding protein 1 (preferred)
PDBe Complex ID:
PDB-CPX-127039 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chromodomain-helicase-DNA-binding protein 1
Molecule details ›
Chains: A, B
Length: 187 amino acids
Theoretical weight: 22.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 187 amino acids
Theoretical weight: 22.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O14646 (Residues: 268-443; Coverage: 10%)
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Chromodomain-helicase-DNA-binding protein 1
Molecule details ›
Chain: C
Length: 115 amino acids
Theoretical weight: 13.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 115 amino acids
Theoretical weight: 13.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: O14646 (Residues: 268-373; Coverage: 6%)
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
C2
Expression system: Escherichia coli BL21(DE3)
