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PDBsum entry 3mp2

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protein metals links
Hydrolase PDB id
3mp2

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
211 a.a. *
Metals
_ZN
Waters ×173
* Residue conservation analysis
PDB id:
3mp2
Name: Hydrolase
Title: Crystal structure of transmissible gastroenteritis virus papain-like protease 1
Structure: Non-structural protein 3. Chain: a. Fragment: unp residues 1071-1281. Synonym: papain-like protease 1. Engineered: yes
Source: Porcine transmissible gastroenteritis coronavirus. Tgev. Organism_taxid: 11151. Strain: purdue. Gene: 1a. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.176     R-free:   0.223
Authors: J.A.Wojdyla,I.Manolaridis,P.A.Tucker
Key ref: J.A.Wojdyla et al. (2010). Papain-like protease 1 from transmissible gastroenteritis virus: crystal structure and enzymatic activity toward viral and cellular substrates. J Virol, 84, 10063-10073. PubMed id: 20668092
Date:
24-Apr-10     Release date:   08-Sep-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0C6V2  (R1A_CVPPU) -  Replicase polyprotein 1a from Porcine transmissible gastroenteritis coronavirus (strain Purdue)
Seq:
Struc:
 
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Seq:
Struc:
4017 a.a.
211 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class 1: E.C.3.4.19.12  - ubiquitinyl hydrolase 1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
   Enzyme class 2: E.C.3.4.22.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
J Virol 84:10063-10073 (2010)
PubMed id: 20668092  
 
 
Papain-like protease 1 from transmissible gastroenteritis virus: crystal structure and enzymatic activity toward viral and cellular substrates.
J.A.Wojdyla, I.Manolaridis, P.B.van Kasteren, M.Kikkert, E.J.Snijder, A.E.Gorbalenya, P.A.Tucker.
 
  ABSTRACT  
 
No abstract given.

 

 

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