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PDBsum entry 2nui

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protein ligands metals links
Hydrolase PDB id
2nui
Jmol
Contents
Protein chain
124 a.a. *
Ligands
BTB
Metals
_CL ×3
Waters ×155
* Residue conservation analysis
PDB id:
2nui
Name: Hydrolase
Title: X-ray structure of synthetic [d83a]rnase a
Structure: Ribonuclease pancreatic. Chain: a. Synonym: rnase 1, rnase a. Engineered: yes. Mutation: yes
Source: Synthetic: yes. Other_details: synthesized using a combination of boc 'in situ neutralization' solid phase peptide synthesis and native chemical ligation. The sequence of the protein is naturally found in bos taurus (bovine).
Resolution:
1.10Å     R-factor:   0.178     R-free:   0.193
Authors: D.J.Boerema,V.A.Tereshko,S.B.H.Kent
Key ref: D.J.Boerema et al. (2008). Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A. Biopolymers, 90, 278-286. PubMed id: 17610259 DOI: 10.1002/bip.20800
Date:
09-Nov-06     Release date:   30-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61823  (RNAS1_BOVIN) -  Ribonuclease pancreatic
Seq:
Struc:
150 a.a.
124 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.1.27.5  - Pancreatic ribonuclease.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   3 terms 
  Biochemical function     protein binding     5 terms  

 

 
DOI no: 10.1002/bip.20800 Biopolymers 90:278-286 (2008)
PubMed id: 17610259  
 
 
Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A.
D.J.Boerema, V.A.Tereshko, S.B.Kent.
 
  ABSTRACT  
 
The total chemical synthesis of RNase A using modern chemical ligation methods is described, illustrating the significant advances that have been made in chemical protein synthesis since Gutte and Merrifield's pioneering preparation of RNase A in 1969. The identity of the synthetic product was confirmed through rigorous characterization, including the determination of the X-ray crystal structure to 1.1 Angstrom resolution.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21365769 C.Wang, Q.X.Guo, and Y.Fu (2011).
Theoretical analysis of the detailed mechanism of native chemical ligation reactions.
  Chem Asian J, 6, 1241-1251.  
20593478 C.Li, X.Li, and W.Lu (2010).
Total chemical synthesis of human T-cell leukemia virus type 1 protease via native chemical ligation.
  Biopolymers, 94, 487-494.  
19404746 U.Arnold (2009).
Incorporation of non-natural modules into proteins: structural features beyond the genetic code.
  Biotechnol Lett, 31, 1129-1139.  
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.