› 3p6y

X-ray diffraction
2.9Å resolution

CF Im25-CF Im68-UGUAA complex

Released:
DOI: 10.2210/pdb3p6y/pdb
PDB entry 3p6y coloured by chain, front view.
PDB entry 3p6y coloured by chain, side view.
PDB entry 3p6y coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Li H, Tong S, Li X, Shi H, Gao Y, Ge H, Niu L, Teng M

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero hexamer
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129135 (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct RNA molecule
Macromolecules (3 distinct):
Cleavage and polyadenylation specificity factor subunit 5 Chains: A, B, E, F, I, J, M, N
Molecule details ›
Chains: A, B, E, F, I, J, M, N
Length: 202 amino acids
Theoretical weight: 23.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43809 (Residues: 34-227; Coverage: 86%)
Gene names: CFIM25, CPSF25, CPSF5, NUDT21
Sequence domains: Nucleotide hydrolase
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Cleavage and polyadenylation specificity factor subunit 6 Chains: C, D, G, H, K, L, O, P
Molecule details ›
Chains: C, D, G, H, K, L, O, P
Length: 90 amino acids
Theoretical weight: 10.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16630 (Residues: 80-161; Coverage: 15%)
Gene names: CFIM68, CPSF6
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits
5'-R(*UP*GP*UP*AP*A)-3' Chains: Q, R, S, T, U, V, W
Molecule details ›
Chains: Q, R, S, T, U, V, W
Length: 5 nucleotides
Theoretical weight: 1.57 KDa

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: 104.783Å b: 129.419Å c: 111.159Å
α: 90° β: 94.01° γ: 90°
R-values:
R R work R free
0.239 0.226 0.275
Expression system: Escherichia coli

Quick links

Citations

18 citation in other articles

Genome-wide analysis of pre-mRNA 3' end processing reveals a decisive role of human cleavage factor I in the regulation of 3' UTR length.
Martin et al. (2012)
17 more

5 mentions without citation

Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.
Xiang et al. (2014)
4 more