2UV4

Crystal Structure of a CBS domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP

Summary for 2UV4

• Entry DOI: 10.2210/pdb2uv4/pdb
• Related: 2UV5 2UV6 2UV7
• Descriptor: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: transferase, cbs domain, lipid synthesis, fatty acid biosynthesis, ampk gamma1 subunit cbs 3 plus 4 amp regulatory subunit
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 17626.10

Authors

Day, P.,Sharff, A.,PArra, L.,Cleasby, A.,Williams, M.,Horer, S.,Nar, H.,Redemann, N.,Tickle, I.,Yon, J. (deposition date: 2007-03-09, release date: 2007-05-08, Last modification date: 2024-05-08)

Primary citation

Day, P.,Sharff, A.,Parra, L.,Cleasby, A.,Williams, M.,Horer, S.,Nar, H.,Redemann, N.,Tickle, I.,Yon, J.
Structure of a Cbs-Domain Pair from the Regulatory Gamma1 Subunit of Human Ampk in Complex with AMP and Zmp.
Acta Crystallogr.,Sect.D, 63:587-, 2007

PubMed Abstract: AMP-activated kinase (AMPK) is central to sensing energy status in eukaryotic cells via binding of AMP and ATP to CBS (cystathionine beta-synthase) domains in the regulatory gamma subunit. The structure of a CBS-domain pair from human AMPK gamma1 in complex with the physiological activator AMP and the pharmacological activator ZMP (AICAR) is presented.

PubMed: 17452784
DOI: 10.1107/S0907444907009110

Experimental method

X-RAY DIFFRACTION (1.33 Å)