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PDBsum entry 4lg8

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protein ligands metals links
DNA binding protein PDB id
4lg8

 

 

 

 

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Contents
Protein chain
310 a.a.
Ligands
UNX ×14
Metals
_NA ×2
Waters ×136
PDB id:
4lg8
Name: DNA binding protein
Title: Crystal structure of prpf19 wd40 repeats
Structure: Pre-mRNA-processing factor 19. Chain: a. Fragment: unp residues 169-504. Synonym: nuclear matrix protein 200, prp19/pso4 homolog, hpso4, senescence evasion factor. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: sf9. Gene: prpf19, nmp200, prp19, snev. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Resolution:
1.89Å     R-factor:   0.158     R-free:   0.197
Authors: C.Xu,W.Tempel,H.He,E.Dobrovetsky,A.Seitova,C.Bountra,C.H.Arrowsmith, A.M.Edwards,J.Min,Structural Genomics Consortium (Sgc)
Key ref: Y.Zhang et al. (2017). Crystal structure of the WD40 domain of human PRPF19. Biochem Biophys Res Commun, 493, 1250-1253. PubMed id: 28962858 DOI: 10.1016/j.bbrc.2017.09.145
Date:
27-Jun-13     Release date:   07-Aug-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UMS4  (PRP19_HUMAN) -  Pre-mRNA-processing factor 19 from Homo sapiens
Seq:
Struc:
504 a.a.
310 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.2.27  - RING-type E3 ubiquitin transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine

 

 
DOI no: 10.1016/j.bbrc.2017.09.145 Biochem Biophys Res Commun 493:1250-1253 (2017)
PubMed id: 28962858  
 
 
Crystal structure of the WD40 domain of human PRPF19.
Y.Zhang, Y.Li, X.Liang, Z.Zhu, H.Sun, H.He, J.Min, S.Liao, Y.Liu.
 
  ABSTRACT  
 
Human Pre-mRNA Processing factor 19 (hPRPF19) is an important component in human spliceosome machinery. hPRPF19 contains a WD40 repeats domain at its C-terminus, which is also conserved in yeast. Here we determined the crystal structure of the C-terminal WD40 repeat domain of hPRPF19 by X-ray crystallography. Our structural analysis revealed some significantly different structure features between the human and yeast Prp19 WD40 repeat domain. However, there are also conserved clusters of residues at the bottom surface of the fourth and the fifth WD40 repeats, which provides the important implication for the conserved Prp19 proteins in both human and yeast.
 

 

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