4riq

X-ray diffraction
2.23Å resolution

Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-189881 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein dpy-30 homolog Chains: A, B, D, E, G, H, J, K, M, N, P, Q, S, T, V, Z
Molecule details ›
Chains: A, B, D, E, G, H, J, K, M, N, P, Q, S, T, V, Z
Length: 56 amino acids
Theoretical weight: 6.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9C005 (Residues: 45-99; Coverage: 56%)
Gene name: DPY30
Sequence domains: Dpy-30 motif
Structure domains: cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain
Set1/Ash2 histone methyltransferase complex subunit ASH2 Chains: C, F, I, L, O, R, U, X
Molecule details ›
Chains: C, F, I, L, O, R, U, X
Length: 27 amino acids
Theoretical weight: 3.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBL3 (Residues: 603-618; Coverage: 3%)
Gene names: ASH2L, ASH2L1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 56.27Å b: 56.27Å c: 95.09Å
α: 90.08° β: 89.9° γ: 115.39°
R-values:
R R work R free
0.243 0.236 0.284
Expression system: Escherichia coli