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PDBsum entry 3zin

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protein ligands Protein-protein interface(s) links
Transport protein/hydrolase PDB id
3zin

 

 

 

 

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Contents
Protein chains
426 a.a.
13 a.a.
Ligands
GLN-LYS-ARG-SER-
PHE-SER
Waters ×188
PDB id:
3zin
Name: Transport protein/hydrolase
Title: Gu_alpha_helicase
Structure: Importin subunit alpha-2. Chain: a. Fragment: residues 72-496. Synonym: importin alpha p1, karyopherin subunit alpha-2, pendulin, pore targeting complex 58 kda subunit, ptac58, rag cohort protein 1, srp1-alpha, importin alpha_ibb. Engineered: yes. Nucleolar RNA helicase 2. Chain: b, c.
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.180     R-free:   0.199
Authors: C.-W.Chang,R.M.Counago,S.J.Williams,B.Kobe
Key ref: C.W.Chang et al. (2013). Distinctive conformation of minor site-specific nuclear localization signals bound to importin-α. Traffic, 14, 1144-1154. PubMed id: 23910026 DOI: 10.1111/tra.12098
Date:
10-Jan-13     Release date:   21-Aug-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P52293  (IMA1_MOUSE) -  Importin subunit alpha-1 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
529 a.a.
426 a.a.
Protein chain
Pfam   ArchSchema ?
Q9JIK5  (DDX21_MOUSE) -  Nucleolar RNA helicase 2 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
851 a.a.
13 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1111/tra.12098 Traffic 14:1144-1154 (2013)
PubMed id: 23910026  
 
 
Distinctive conformation of minor site-specific nuclear localization signals bound to importin-α.
C.W.Chang, R.M.Couñago, S.J.Williams, M.Bodén, B.Kobe.
 
  ABSTRACT  
 
No abstract given.

 

 

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