Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism.
about
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in natureConverting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C)Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanismCrystal structure of D-stereospecific amidohydrolase from Streptomyces sp. 82F2 - insight into the structural factors for substrate specificityUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationThe "tale" of UmuD and its role in SOS mutagenesis.Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavageEndopeptidase activity characterization of E. coli-derived infectious bursal disease virus protein 4 tubules.CASTp: Computed Atlas of Surface Topography of proteins.Multiple strategies for translesion synthesis in bacteriaGetting intimate with trypsin, the leading protease in proteomics.The Roles of UmuD in Regulating Mutagenesis.
P2860
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P2860
Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@en
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@nl
type
label
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@en
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@nl
prefLabel
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@en
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@nl
P2860
P356
P1433
P1476
Common protein architecture an ...... zing a Ser/Lys dyad mechanism.
@en
P2093
Strynadka NC
P2860
P304
P356
10.1110/PS.8.11.2533
P577
1999-11-01T00:00:00Z