› 4lg8

X-ray diffraction
1.89Å resolution

Crystal structure of PRPF19 WD40 repeats

Released:
DOI: 10.2210/pdb4lg8/pdb
PDB entry 4lg8 coloured by chain, front view.
PDB entry 4lg8 coloured by chain, side view.
PDB entry 4lg8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the WD40 domain of human PRPF19.
Zhang Y, Li Y, Liang X, Zhu Z, Sun H, He H, Min J, Liao S, Liu Y
Biochem Biophys Res Commun 493 1250-1253 (2017)
PMID: 28962858

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pre-mRNA-processing factor 19 Chain: A
Molecule details ›
Chain: A
Length: 354 amino acids
Theoretical weight: 39.06 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9UMS4 (Residues: 169-504; Coverage: 67%)
Gene names: NMP200, PRP19, PRPF19, SNEV
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand UNX 14 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P3121
Unit cell:
a: 83.055Å b: 83.055Å c: 75.533Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.156 0.197
Expression system: Spodoptera frugiperda

Quick links

Citations

1 citations in other articles

Non-TZF Protein AtC3H59/ZFWD3 Is Involved in Seed Germination, Seedling Development, and Seed Development, Interacting with PPPDE Family Protein Desi1 in Arabidopsis.
Seok et al. (2021)

5 mentions without citation

The PRP19 Ubiquitin Ligase, Standing at the Cross-Roads of mRNA Processing and Genome Stability.
Idrissou et al. (2022)
4 more