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1S5O

Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase

Summary for 1S5O
Entry DOI10.2210/pdb1s5o/pdb
Descriptorcarnitine acetyltransferase isoform 2, CARNITINE (3 entities in total)
Functional Keywordscarnitine acetyltransferase, binary complex, steady-state enzyme kinetics, substrate binding site, transferase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum (Potential). Isoform 1: Mitochondrion (Potential). Isoform 2: Peroxisome (Potential): P43155
Total number of polymer chains1
Total formula weight70065.07
Authors
Govindasamy, L.,Kukar, T.,Lian, W.,Pedersen, B.,Gu, Y.,Agbandje-Mckenna, M.,Jin, S.,Mckenna, R.,Wu, D. (deposition date: 2004-01-21, release date: 2004-02-03, Last modification date: 2023-08-23)
Primary citationGovindasamy, L.,Kukar, T.,Lian, W.,Pedersen, B.,Gu, Y.,Agbandje-McKenna, M.,Jin, S.,McKenna, R.,Wu, D.
Structural and mutational characterization of l-carnitine binding to human carnitine acetyltransferase.
J.Struct.Biol., 146:416-424, 2004
Cited by
PubMed: 15099582
DOI: 10.1016/j.jsb.2004.01.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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