4nad

X-ray diffraction
2.8Å resolution

Crystal Structure of the C-terminal Domain of CREPT

Released:
Source organism: Homo sapiens
Entry authors: Mei K, Jin Z, Ren F, Wang Y

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulation of nuclear pre-mRNA domain-containing protein 1B Chains: A, B
Molecule details ›
Chains: A, B
Length: 154 amino acids
Theoretical weight: 17.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NQG5 (Residues: 177-326; Coverage: 46%)
Gene names: C20orf77, CREPT, RPRD1B
Sequence domains: Cell-cycle alteration and expression-elevated protein in tumour
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 33.28Å b: 55.66Å c: 84.45Å
α: 90° β: 92.9° γ: 90°
R-values:
R R work R free
0.24 0.237 0.29
Expression system: Escherichia coli