4jk8

X-ray diffraction
1.15Å resolution

Open and closed forms of R1865A human PRP8 RNase H-like domain with bound Mg ion

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pre-mRNA-processing-splicing factor 8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 222 amino acids
Theoretical weight: 25.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6P2Q9 (Residues: 1769-1990; Coverage: 10%)
Gene names: PRPC8, PRPF8
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 76.198Å b: 78.037Å c: 94.063Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.14 0.16
Expression system: Escherichia coli BL21(DE3)