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PDBsum entry 3o2q

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3o2q
Jmol
Contents
Protein chains
317 a.a. *
189 a.a. *
Ligands
PRO-THR-SEP-PRO-
SER-TYR
PO4
Waters ×250
* Residue conservation analysis
PDB id:
3o2q
Name: Hydrolase
Title: Crystal structure of the human symplekin-ssu72-ctd phosphope complex
Structure: Symplekin. Chain: a, d. Fragment: n-terminal domain. Engineered: yes. RNA polymerase ii subunit a c-terminal domain pho ssu72. Chain: b, e. Synonym: ctd phosphatase ssu72. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sympk, spk. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ssu72, hspc182, pnas-120. Synthetic: yes
Resolution:
2.40Å     R-factor:   0.187     R-free:   0.242
Authors: L.Tong,K.Xiang
Key ref: K.Xiang et al. (2010). Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex. Nature, 467, 729-733. PubMed id: 20861839
Date:
22-Jul-10     Release date:   06-Oct-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q92797  (SYMPK_HUMAN) -  Symplekin
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1274 a.a.
317 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9NP77  (SSU72_HUMAN) -  RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Seq:
Struc:
194 a.a.
189 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains B, E: E.C.3.1.3.16  - Protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [a protein]-serine/threonine phosphate + H2O = [a protein]- serine/threonine + phosphate
[a protein]-serine/threonine phosphate
+ H(2)O
= [a protein]- serine/threonine
+
phosphate
Bound ligand (Het Group name = SEP)
matches with 50.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     dephosphorylation of RNA polymerase II C-terminal domain   3 terms 
  Biochemical function     protein binding     4 terms  

 

 
    Key reference    
 
 
Nature 467:729-733 (2010)
PubMed id: 20861839  
 
 
Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex.
K.Xiang, T.Nagaike, S.Xiang, T.Kilic, M.M.Beh, J.L.Manley, L.Tong.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21292162 S.Danckwardt, A.S.Gantzert, S.Macher-Goeppinger, H.C.Probst, M.Gentzel, M.Wilm, H.J.Gröne, P.Schirmacher, M.W.Hentze, and A.E.Kulozik (2011).
p38 MAPK controls prothrombin expression by regulated RNA 3' end processing.
  Mol Cell, 41, 298-310.  
21329879 T.Nagaike, C.Logan, I.Hotta, O.Rozenblatt-Rosen, M.Meyerson, and J.L.Manley (2011).
Transcriptional activators enhance polyadenylation of mRNA precursors.
  Mol Cell, 41, 409-418.  
21204787 Y.Zhang, M.Zhang, and Y.Zhang (2011).
Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue.
  Biochem J, 434, 435-444.
PDB codes: 3omw 3omx
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.