PDBe 5f5s

X-ray diffraction
2.4Å resolution

Crystal structure of the Prp38-MFAP1 complex of Homo sapiens

Released:
Source organism: Homo sapiens
Primary publication:
Scaffolding in the Spliceosome via Single α Helices.
Structure 24 1972-1983 (2016)
PMID: 27773687

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pre-mRNA-splicing factor 38A Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 21.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8NAV1 (Residues: 1-179; Coverage: 57%)
Gene name: PRPF38A
Sequence domains: PRP38 family
Microfibrillar-associated protein 1 Chain: B
Molecule details ›
Chain: B
Length: 80 amino acids
Theoretical weight: 9.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55081 (Residues: 267-344; Coverage: 18%)
Gene name: MFAP1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P6122
Unit cell:
a: 66.79Å b: 66.79Å c: 242.54Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.221 0.261
Expression system: Escherichia coli BL21(DE3)