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PDBsum entry 3n4p
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protein metals Protein-protein interface(s) links
DNA binding protein PDB id
3n4p

 

 

 

 

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Contents
Protein chains
216 a.a. *
227 a.a. *
Metals
_MG ×7
Waters ×98
* Residue conservation analysis
PDB id:
3n4p
Name: DNA binding protein
Title: Human cytomegalovirus terminase nuclease domain
Structure: Terminase subunit ul89 protein. Chain: a, b, c, d. Fragment: unp residues 418-674. Engineered: yes
Source: Human herpesvirus 5. Organism_taxid: 10363. Strain: towne. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.15Å     R-factor:   0.222     R-free:   0.272
Authors: M.Nadal,P.J.Mas,A.G.Blanco,C.Arnan,M.Sola,D.J.Hart,M.Coll
Key ref: M.Nadal et al. (2010). Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain. Proc Natl Acad Sci U S A, 107, 16078-16083. PubMed id: 20805464
Date:
22-May-10     Release date:   06-Oct-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16732  (TRM3_HCMVA) -  Tripartite terminase subunit 3 from Human cytomegalovirus (strain AD169)
Seq:
Struc: 		 
Seq:
Struc: 		674 a.a.
216 a.a.
Protein chains
Pfam   ArchSchema ?
P16732  (TRM3_HCMVA) -  Tripartite terminase subunit 3 from Human cytomegalovirus (strain AD169)
Seq:
Struc: 		 
Seq:
Struc: 		674 a.a.
227 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Proc Natl Acad Sci U S A 107:16078-16083 (2010)
PubMed id: 20805464  
 
 
Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain.
M.Nadal, P.J.Mas, P.J.Mas, A.G.Blanco, C.Arnan, M.Solà, D.J.Hart, M.Coll.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21109524 M.Ghosh-Kumar, T.I.Alam, B.Draper, J.D.Stack, and V.B.Rao (2011).
Regulation by interdomain communication of a headful packaging nuclease from bacteriophage T4.
  Nucleic Acids Res, 39, 2742-2755.  
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.

 

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