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PDBsum entry 3nc1

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protein ligands metals Protein-protein interface(s) links
Gtp-binding protein/transport protein PDB id
3nc1

 

 

 

 

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Contents
Protein chains
173 a.a. *
1026 a.a. *
Ligands
GTP
Metals
_MG
* Residue conservation analysis
PDB id:
3nc1
Name: Gtp-binding protein/transport protein
Title: Crystal structure of the crm1-rangtp complex
Structure: Gtp-binding nuclear protein ran. Chain: c. Synonym: gtpase ran, ras-related nuclear protein, ras-like protein tc4, androgen receptor-associated protein 24. Engineered: yes. Mutation: yes. Exportin-1. Chain: a. Synonym: exp1, chromosome region maintenance 1 protein homolog.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ara24, ok/sw-cl.81, ran, ran (geneid: 5901). Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.
Resolution:
3.35Å     R-factor:   0.221     R-free:   0.254
Authors: T.Guttler,T.Madl,P.Neumann,D.Deichsel,L.Corsini,T.Monecke,R.Ficner, M.Sattler,D.Gorlich
Key ref: T.Güttler et al. (2010). NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nat Struct Biol, 17, 1367-1376. PubMed id: 20972448
Date:
04-Jun-10     Release date:   27-Oct-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62826  (RAN_HUMAN) -  GTP-binding nuclear protein Ran from Homo sapiens
Seq:
Struc:
216 a.a.
173 a.a.*
Protein chain
Pfam   ArchSchema ?
Q6P5F9  (XPO1_MOUSE) -  Exportin-1 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1071 a.a.
1026 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: Chain A: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chain C: E.C.3.6.5.-  - ?????
[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.

 

 
Nat Struct Biol 17:1367-1376 (2010)
PubMed id: 20972448  
 
 
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
T.Güttler, T.Madl, P.Neumann, D.Deichsel, L.Corsini, T.Monecke, R.Ficner, M.Sattler, D.Görlich.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21364925 K.Langer, C.Dian, V.Rybin, C.W.Müller, and C.Petosa (2011).
Insights into the Function of the CRM1 Cofactor RanBP3 from the Structure of Its Ran-Binding Domain.
  PLoS One, 6, e17011.
PDB codes: 2y8f 2y8g
21088665 I.W.Mattaj, and C.W.Müller (2010).
Solving the NES problem.
  Nat Struct Mol Biol, 17, 1288-1289.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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