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PDBsum entry 5hiz

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protein Protein-protein interface(s) links
RNA binding protein PDB id
5hiz

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
96 a.a.
PDB id:
5hiz
Name: RNA binding protein
Title: The structure of pedv nsp9
Structure: Non-structural protein 9. Chain: a, b. Synonym: nsp9. Engineered: yes
Source: Porcine epidemic diarrhea virus cv777. Pedv. Organism_taxid: 229032. Strain: cv777. Gene: rep, 1a-1b. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768.
Resolution:
2.90Å     R-factor:   0.272     R-free:   0.334
Authors: F.Deng,G.Peng
Key ref: f.deng and g.peng (2018). Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity. J.Virol., 92, . PubMed id: 29925659
Date:
12-Jan-16     Release date:   25-Jan-17    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0C6Y4  (R1AB_PEDV7) -  Replicase polyprotein 1ab from Porcine epidemic diarrhea virus (strain CV777)
Seq:
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Seq:
Struc:
6781 a.a.
96 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.2.1.1.56  - mRNA (guanine-N(7))-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L- methionine
= 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L-homocysteine
   Enzyme class 2: E.C.2.1.1.57  - methyltransferase cap1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H+
5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L-methionine
= 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA
+ S-adenosyl-L-homocysteine
+ H(+)
   Enzyme class 3: E.C.2.7.7.48  - RNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA(n)
+ ribonucleoside 5'-triphosphate
= RNA(n+1)
+ diphosphate
   Enzyme class 4: E.C.2.7.7.50  - mRNA guanylyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
5'-end diphospho-ribonucleoside in mRNA
+ GTP
+ H(+)
= 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA
+ diphosphate
   Enzyme class 5: E.C.3.1.13.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 6: 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 7: E.C.3.4.22.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 8: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
   Enzyme class 9: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
   Enzyme class 10: E.C.4.6.1.-  - ?????
[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.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J.Virol. 92: (2018)
PubMed id: 29925659  
 
 
Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity.
f.deng, g.peng.
 
  ABSTRACT  
 
No abstract given.

 

 

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