![]() | Class d: Alpha and beta proteins (a+b) [53931] (279 folds) |
![]() | Fold d.153: Ntn hydrolase-like [56234] (2 superfamilies) 4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing |
![]() | Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (5 families) ![]() N-terminal residue provides two catalytic groups, nucleophile and proton donor |
![]() | Family d.153.1.5: (Glycosyl)asparaginase [56261] (1 protein) |
![]() | Protein Glycosylasparaginase (aspartylglucosaminidase, AGA) [56262] (3 species) the precursor chain is cleaved onto 2 fragments by autoproteolysis |
![]() | Species Escherichia coli [TaxId:562] [103315] (3 PDB entries) isoaspartyl peptidase with L-asparaginase activity putative L-asparaginase YbiK |
![]() | Domain d1t3m.2: 1t3m C:,D: [106362] |
PDB Entry: 1t3m (more details), 1.65 Å
SCOP Domain Sequences for d1t3m.2:
Sequence; same for both SEQRES and ATOM records: (download)
>g1t3m.2 d.153.1.5 (C:,D:) Glycosylasparaginase (aspartylglucosaminidase, AGA) {Escherichia coli} kaviaihggagaisraqmslqqelryiealsaivetgqkmleagesaldvvteavrllee cplfnagigavftrdetheldacvmdgntlkagavagvshlrnpvlaarlvmeqsphvmm igegaenfafargmervspeifstslryeqllaarkXtvgavaldldgnlaaatstggmt nklpgrvgdsplvgagcyannasvavsctgtgevfiralaaydiaalmdygglslaeace rvvmeklpalggsggliaidhegnvalpfntegmyrawgyagdtpttgiyr
Timeline for d1t3m.2:
![]() Domains from other chains: (mouse over for more information) d1t3m.1, d1t3m.1, d1t3m.1, d1t3m.1 |