Literature summary for 3.5.4.38 extracted from

Hou, S.; Silvas, T.V.; Leidner, F.; Nalivaika, E.A.; Matsuo, H.; Kurt Yilmaz, N.; Schiffer, C.A.
Structural analysis of the active site and DNA binding of human cytidine deaminase APOBEC3B (2019), J. Chem. Theory Comput., 15, 637-647 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of structure. Residue Arg211 in loop 1 is the gatekeeper coordinating DNA. ssDNA binds to the C-terminal domain in a U-shape, and loop 1 undergoes major conformational changes to open up the active site for DNA binding. Residue D314 defines substrate specificity for thymidine over cytidine at -1 position. An auto-inhibited conformation in the C-terminal domain restricts access and binding of DNA to the active site	Homo sapiens

Crystallization (Comment)

Organism

modeling of structure. Residue Arg211 in loop 1 is the gatekeeper coordinating DNA. ssDNA binds to the C-terminal domain in a U-shape, and loop 1 undergoes major conformational changes to open up the active site for DNA binding. Residue D314 defines substrate specificity for thymidine over cytidine at -1 position. An auto-inhibited conformation in the C-terminal domain restricts access and binding of DNA to the active site

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9UH17	-	-

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Release 2023.1 (January 2023)