Literature summary for 6.5.1.1 extracted from

Thermococcus sp.Petrova, T.; Bezsudnova, E.Y.; Boyko, K.M.; Mardanov, A.V.; Polyakov, K.M.; Volkov, V.V.; Kozin, M.; Ravin, N.V.; Shabalin, I.G.; Skryabin, K.G.; Stekhanova, T.N.; Kovalchuk, M.V.; Popov, V.O.
ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain (2012), Acta Crystallogr. Sect. F, 68, 1440-1447.

Search for more literature for 6.5.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Thermococcus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
results of a crystallographic study of the ATP-dependent DNA ligase from Thermococcus sp. 1519 with all three domains (N-terminal DNA-binding domain (DBD), an adenylation domain (AdD) and a C-terminal OB-fold domain (OBD)) are reported	Thermococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Thermococcus sp.	C0LJI8	-	-

Synonyms

Synonyms	Comment	Organism
DNA ligase	-	Thermococcus sp.
LigTh1519	-	Thermococcus sp.

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)