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3P0J

Leishmania major Tyrosyl-tRNA synthetase in complex with tyrosinol, triclinic crystal form 1

Summary for 3P0J
Entry DOI10.2210/pdb3p0j/pdb
Related3P0H 3P0I
DescriptorTyrosyl-tRNA synthetase, 4-[(2S)-2-amino-3-hydroxypropyl]phenol, SODIUM ION (3 entities in total)
Functional Keywordsaminoacyl-trna synthetase, trna ligase, aars, tyrrs, pseudodimer, translation, atp-binding, nucleotide-binding, ligase, structural genomics, medical structural genomics of pathogenic protozoa, msgpp
Biological sourceLeishmania major
Total number of polymer chains4
Total formula weight305004.33
Authors
Larson, E.T.,Merritt, E.A.,Medical Structural Genomics of Pathogenic Protozoa (MSGPP) (deposition date: 2010-09-28, release date: 2011-03-23, Last modification date: 2023-12-06)
Primary citationLarson, E.T.,Kim, J.E.,Castaneda, L.J.,Napuli, A.J.,Zhang, Z.,Fan, E.,Zucker, F.H.,Verlinde, C.L.,Buckner, F.S.,Van Voorhis, W.C.,Hol, W.G.,Merritt, E.A.
The Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer.
J.Mol.Biol., 409:159-176, 2011
Cited by
PubMed: 21420975
DOI: 10.1016/j.jmb.2011.03.026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.89 Å)
Structure validation

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