SCOPe 2.08: Domain d1llwa3: 1llw A:1-422

Lineage for d1llwa3 (1llw A:1-422)

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.153.1.1: Class II glutamine amidotransferases [56236] (6 proteins)
   has slightly different topology than other families do

6. Protein Alpha subunit of glutamate synthase, N-terminal domain [69833] (2 species)

7. Species Synechocystis sp. [TaxId:1143] [75566] (5 PDB entries)

8. Domain d1llwa3: 1llw A:1-422 [74019]
   Other proteins in same PDB: d1llwa1, d1llwa2
   complexed with akg, f3s, fmn
   has additional subdomain(s) that are not in the common domain

Details for d1llwa3

PDB Entry: 1llw, 2.7 Å

PDB Description: Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

PDB Compounds: (A:) Ferredoxin-dependent glutamate synthase

SCOPe Domain Sequences for d1llwa3:

Sequence; same for both SEQRES and ATOM records:

>d1llwa3 d.153.1.1 (A:1-422) Alpha subunit of glutamate synthase, N-terminal domain {Synechocystis sp. [TaxId: 1143]}
cgvgfianlrgkpdhtlveqalkalgcmehrggcsadndsgdgagvmtaiprellaqwfn
trnlpmpdgdrlgvgmvflpqepsarevarayveevvrlekltvlgwrevpvnsdvlgiq
aknnqphieqilvtcpegcagdeldrrlyiarsiigkklaedfyvcsfscrtivykgmvr
siilgefyldlknpgytsnfavyhrrfstntmpkwplaqpmrllghngeintllgninwm
aarekelevsgwtkaelealtpivnqansdsynldsalellvrtgrspleaamilvpeay
knqpalkdypeisdfhdyysglqepwdgpallvfsdgkivgagldrnglrparycitkdd
yivlgseagvvdlpevdivekgrlapgqmiavdlaeqkilknyqikqqaaqkypygewik
iq

Timeline for d1llwa3:

• d1llwa3 first appeared in SCOP 1.61
  
• d1llwa3 appears in SCOPe 2.07