![]() | Class d: Alpha and beta proteins (a+b) [53931] (260 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] (2 PDB entries) putative L-asparaginase YbiK |
![]() | Domain d1k2x.2: 1k2x C:,D: [90930] complexed with cl, na |
PDB Entry: 1k2x (more details), 1.65 Å
SCOP Domain Sequences for d1k2x.2:
Sequence; same for both SEQRES and ATOM records: (download)
>g1k2x.2 d.153.1.5 (C:,D:) Glycosylasparaginase (aspartylglucosaminidase, AGA) {Escherichia coli} gkaviaihggagaisraqmslqqelryiealsaivetgqkmleagesaldvvteavrlle ecplfnagigavftrdetheldacvmdgntlkagavagvshlrnpvlaarlvmeqsphvm migegaenfafargmervspeifstslryeqllaarXtvgavaldldgnlaaatstggmt nklpgrvgdsplvgagcyannasvavsctgtgevfiralaaydiaalmdygglslaeace rvvmeklpalggsggliaidhegnvalpfntegmyrawgyagdtpttgiyre
Timeline for d1k2x.2:
![]() Domains from other chains: (mouse over for more information) d1k2x.1, d1k2x.1, d1k2x.1, d1k2x.1 |