SCOPe 2.08: Domain d2dbx.1: 2dbx A:37-387,B:391-580

Lineage for d2dbx.1 (2dbx A:37-387,B:391-580)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.153: Ntn hydrolase-like [56234] (2 superfamilies)
   4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing

4. Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families)
   N-terminal residue provides two catalytic groups, nucleophile and proton donor

5. Family d.153.1.6: Gamma-glutamyltranspeptidase-like [143906] (4 proteins)
   Pfam PF01019

6. Protein Gamma-glutamyltranspeptidase, GGT [143911] (2 species)

7. Species Escherichia coli [TaxId:562] [143913] (7 PDB entries)
   Uniprot P18956 29-387,391-580! Uniprot P18956 29-580

8. Domain d2dbx.1: 2dbx A:37-387,B:391-580 [131363]
   mature cleaved protein
   complexed with ca, glu, gol

Details for d2dbx.1

PDB Entry: 2dbx, 1.7 Å

PDB Description: Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Complexed with L-Glutamate

PDB Compounds: (A:) Gamma-glutamyltranspeptidase, (B:) Gamma-glutamyltranspeptidase

SCOPe Domain Sequences for d2dbx.1:

Sequence; same for both SEQRES and ATOM records:

>g2dbx.1 d.153.1.6 (A:37-387,B:391-580) Gamma-glutamyltranspeptidase, GGT {Escherichia coli [TaxId: 562]}
eedvfhpvrakqgmvasvdatatqvgvdilkeggnavdaavavgyalavthpqagnlggg
gfmlirskngnttaidfremapakatrdmflddqgnpdskksltshlasgtpgtvagfsl
aldkygtmplnkvvqpafklardgfivndaladdlktygsevlpnhenskaifwkegepl
kkgdtlvqanlakslemiaengpdefykgtiaeqiaqemqkngglitkedlaaykavert
pisgdyrgyqvysmpppssggihivqilnilenfdmkkygfgsadamqimaeaekyayad
rseylgdpdfvkvpwqaltnkayaksiadqidinkakpsseirpgklapyeXtthysvvd
kdgnavavtytlnttfgtgivagesgillnnqmddfsakpgvpnvyglvggdanavgpnk
rplssmsptivvkdgktwlvtgspggsriittvlqmvvnsidyglnvaeatnaprfhhqw
lpdelrvekgfspdtlklleakgqkvalkeamgstqsimvgpdgelygasdprsvddlta
gy

Timeline for d2dbx.1:

• d2dbx.1 first appeared in SCOP 1.73
  
• d2dbx.1 appears in SCOPe 2.07