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Structure paper

TitleStructure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.
Journal, issue, pagesStructure, Vol. 17, Page 128-138, Year 2009
Publish dateJun 28, 2007 (structure data deposition date)
AuthorsScheeff, E.D. / Eswaran, J. / Bunkoczi, G. / Knapp, S. / Manning, G.
External linksStructure / PubMed:19141289
MethodsX-ray diffraction
Resolution1.7 - 2 Å
Structure data

PDB-2jii:
Structure of vaccinia related kinase 3
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2v62:
Structure of vaccinia-related kinase 2
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-SIN:
SUCCINIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PSEUDO KINASE DOMAIN / VACCINIA RELATED KINASE / SERINE/THREONINE-PROTEIN KINASE / VRK3 / KINASE / ATP-BINDING / NUCLEOTIDE-BINDING / MEMBRANE / TRANSMEMBRANE

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