spacer
spacer

PDBsum entry 1lfn

Go to PDB code: 
protein links
Transferase PDB id
1lfn

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
305 a.a.
Theoretical model
PDB id:
1lfn
Name: Transferase
Title: Theoretical structure of human-cyclin dependent kinase 3 (cdk3)
Structure: Cell division protein kinase 3. Chain: a. Synonym: cyclin-dependent kinase 3, cdk3. Ec: 2.7.1.-
Source: Homo sapiens. Human
Authors: K.Narayana,T.Rajasekhar,J.A.R.P.Sarma
Key ref: G.E.Norris et al. (1991). Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change. Acta Crystallogr B, 47, 998. PubMed id: 1772635
Date:
11-Apr-02     Release date:   24-Apr-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q00526  (CDK3_HUMAN) -  Cyclin-dependent kinase 3
Seq:
Struc:
305 a.a.
305 a.a.
Key:    PfamA domain  Secondary structure

 

 
Acta Crystallogr B 47:998 (1991)
PubMed id: 1772635  
 
 
Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.
G.E.Norris, B.F.Anderson, E.N.Baker.
 
  ABSTRACT  
 
The crystal structure of an orthorhombic form of human apolactoferrin (ApoLf) has been determined from 2.8 A diffractometer data by molecular replacement methods. A variety of search models derived from the diferric lactoferrin structure (Fe2Lf) were used to obtain a consistent solution to the rotation function. An R-factor search gave the correct translational solution and the model was refined by rigid-body least-squares refinement (program CORELS). Only three of the four domains were located correctly by this procedure, however; the fourth was finally placed correctly by rotating it manually onto three strands of electron density which were recognized as part of its central beta-sheet. The final model, refined by restrained least-squares methods to an R factor of 0.214 for data in the resolution range 10.0 to 2.8 A, shows a large domain movement in the N-terminal half of the molecule (a 54 degree rotation of domain N2) and smaller domain movements elsewhere, when compared with Fe2Lf. A feature of the crystal structure is that although the ApoLf and Fe2Lf unit cells appear very similar, their crystal packing and molecular structures are quite different.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18433058 S.C.Flores, K.S.Keating, J.Painter, F.Morcos, K.Nguyen, E.A.Merritt, L.A.Kuhn, and M.B.Gerstein (2008).
HingeMaster: normal mode hinge prediction approach and integration of complementary predictors.
  Proteins, 73, 299-319.  
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.

 

spacer

spacer