SCOPe 2.08: Domain d2dg5.2: 2dg5 C:37-387,D:391-580

Lineage for d2dg5.2 (2dg5 C:37-387,D: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 d2dg5.2: 2dg5 C:37-387,D:391-580 [131501]
   mature cleaved protein
   complexed with ca, glu, gol

Details for d2dg5.2

PDB Entry: 2dg5, 1.6 Å

PDB Description: crystal structure of gamma-glutamyl transpeptidase from escherichia coli in complex with hydrolyzed glutathione

PDB Compounds: (C:) Gamma-glutamyltranspeptidase, (D:) Gamma-glutamyltranspeptidase

SCOPe Domain Sequences for d2dg5.2:

Sequence; same for both SEQRES and ATOM records:

>g2dg5.2 d.153.1.6 (C:37-387,D:391-580) Gamma-glutamyltranspeptidase, GGT {Escherichia coli [TaxId: 562]}
eedvfhpvrakqgmvasvdatatqvgvdilkeggnavdaavavgyalavthpqagnlggg
gfmlirskngnttaidfremapakatrdmflddqgnpdskksltshlasgtpgtvagfsl
aldkygtmplnkvvqpafklardgfivndaladdlktygsevlpnhenskaifwkegepl
kkgdtlvqanlakslemiaengpdefykgtiaeqiaqemqkngglitkedlaaykavert
pisgdyrgyqvysmpppssggihivqilnilenfdmkkygfgsadamqimaeaekyayad
rseylgdpdfvkvpwqaltnkayaksiadqidinkakpsseirpgklapyeXtthysvvd
kdgnavavtytlnttfgtgivagesgillnnqmddfsakpgvpnvyglvggdanavgpnk
rplssmsptivvkdgktwlvtgspggsriittvlqmvvnsidyglnvaeatnaprfhhqw
lpdelrvekgfspdtlklleakgqkvalkeamgstqsimvgpdgelygasdprsvddlta
gy

Timeline for d2dg5.2:

• d2dg5.2 first appeared in SCOP 1.73
  
• d2dg5.2 appears in SCOPe 2.07