Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Nucleosome, Histone (preferred)
PDBe Complex ID:
PDB-CPX-179453 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone H3-like centromeric protein CSE4
Molecule details ›
Chains: A, C, E, G
Length: 92 amino acids
Theoretical weight: 10.75 KDa
Source organism: Kluyveromyces lactis NRRL Y-1140
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Length: 92 amino acids
Theoretical weight: 10.75 KDa
Source organism: Kluyveromyces lactis NRRL Y-1140
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q6CTI2 (Residues: 93-184; Coverage: 50%)
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4
Molecule details ›
Chains: B, D, F, H
Length: 103 amino acids
Theoretical weight: 11.44 KDa
Source organism: Kluyveromyces lactis NRRL Y-1140
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
Length: 103 amino acids
Theoretical weight: 11.44 KDa
Source organism: Kluyveromyces lactis NRRL Y-1140
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q6CMU6 (Residues: 1-103; Coverage: 100%)
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 24-ID-E
Spacegroup:
R3
Expression system: Escherichia coli BL21(DE3)
