Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate (Q27653555)
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Current Data About Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate
(P31) (Q13442814)

(P50) (Q28037032)
(P1545) 3

(P304) 555-63

(P407) (Q1860)

(P433) 5

(P478) 145

(P577) +2009-05-00T00:00:00Z

(P921) (Q895901)

(Q20980558)
(P1932) Bacillus stearothermophilus
(P887)

(P1433) (Q6294839)

(P1476) "Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate" (language: en)

(P2093) Haruko Sakurama
(P1545) 1

Teisuke Takita
(P1545) 2

Takafumi Itoh
(P1545) 4

Kiyoshi Yasukawa
(P1545) 5

Kuniyo Inouye
(P1545) 6

(P2860) (Q26778405)
(P248)
(P813) Friday, May 20, 2022
(P854) https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

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External Links
(P356) 10.1093/JB/MVP014
(P698) 19174549
(P8608) release_tgvndmhmejhjnggz234cbj74iu