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PDBsum entry 4j1v

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protein ligands metals Protein-protein interface(s) links
Peptide binding protein/viral protein PDB id
4j1v

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
166 a.a.
15 a.a.
Ligands
ALA-LEU-PRO-ALA-
TRP-ALA-ARG-PRO-
ASP
×2
Metals
_ZN ×2
Waters ×386
PDB id:
4j1v
Name: Peptide binding protein/viral protein
Title: Functional and structural studies of mobkl1b, a salvador/warts/hippo tumor suppressor pathway, in hcv replication
Structure: Mob kinase activator 1a. Chain: a, c. Synonym: mob1 alpha, mob1a, mob1 homolog 1b, mps one binder kinase activator-like 1b. Engineered: yes. Ns5a domain ii peptide. Chain: e, g, f, h. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mob1a, c2orf6, mob4b, mobk1b, mobkl1b. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Hepatitis c virus. Hcv.
Resolution:
1.95Å     R-factor:   0.196     R-free:   0.225
Authors: H.-Y.Chung,M.Gu,C.M.Rice
Key ref: H.Y.Chung et al. (2014). Seed sequence-matched controls reveal limitations of small interfering RNA knockdown in functional and structural studies of hepatitis C virus NS5A-MOBKL1B interaction. J Virol, 88, 11022-11033. PubMed id: 25031347 DOI: 10.1128/JVI.01582-14
Date:
02-Feb-13     Release date:   06-Aug-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H8S9  (MOB1A_HUMAN) -  MOB kinase activator 1A from Homo sapiens
Seq:
Struc:
216 a.a.
166 a.a.
Protein chains
Pfam   ArchSchema ?
Q99IB8  (POLG_HCVJF) -  Genome polyprotein from Hepatitis C virus genotype 2a (isolate JFH-1)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
3033 a.a.
15 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: Chains G, H: 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 3: Chains G, H: E.C.3.4.21.98  - hepacivirin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
   Enzyme class 4: Chains G, H: E.C.3.4.22.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 5: Chains G, H: E.C.3.6.1.15  - nucleoside-triphosphate phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
ribonucleoside 5'-triphosphate
+ H2O
= ribonucleoside 5'-diphosphate
+ phosphate
+ H(+)
   Enzyme class 6: Chains G, H: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
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    
 
 
DOI no: 10.1128/JVI.01582-14 J Virol 88:11022-11033 (2014)
PubMed id: 25031347  
 
 
Seed sequence-matched controls reveal limitations of small interfering RNA knockdown in functional and structural studies of hepatitis C virus NS5A-MOBKL1B interaction.
H.Y.Chung, M.Gu, E.Buehler, M.R.MacDonald, C.M.Rice.
 
  ABSTRACT  
 
No abstract given.

 

 

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