SCOP 1.63: Domain d1derg1: 1der G:2-136,G:410-526

Lineage for d1derg1 (1der G:2-136,G:410-526)

1. Root: SCOP 1.63

2. Class a: All alpha proteins [46456] (171 folds)

3. Fold a.129: GroEL equatorial domain-like chaperone equatorial domain [48591] (1 superfamily)
   multihelical; 8 helices arranged in 2 parallel layers

4. Superfamily a.129.1: GroEL equatorial domain-like chaperone equatorial domain [48592] (2 families)
   duplication: two 4-helical subdomains are related by a pseudodyad passing through the ATP-binding site

5. Family a.129.1.1: GroEL chaperone, ATPase domain [48593] (1 protein)

6. Protein GroEL, E domain [48594] (2 species)

7. Species Escherichia coli [TaxId:562] [48595] (4 PDB entries)

8. Domain d1derg1: 1der G:2-136,G:410-526 [19465]
   Other proteins in same PDB: d1dera2, d1dera3, d1derb2, d1derb3, d1derc2, d1derc3, d1derd2, d1derd3, d1dere2, d1dere3, d1derf2, d1derf3, d1derg2, d1derg3, d1derh2, d1derh3, d1deri2, d1deri3, d1derj2, d1derj3, d1derk2, d1derk3, d1derl2, d1derl3, d1derm2, d1derm3, d1dern2, d1dern3

Details for d1derg1

PDB Entry: 1der, 2.4 Å

PDB Description: the 2.4 angstrom crystal structure of the bacterial chaperonin groel complexed with atp-gamma-s

SCOP Domain Sequences for d1derg1:

Sequence; same for both SEQRES and ATOM records:

>d1derg1 a.129.1.1 (G:2-136,G:410-526) GroEL, E domain {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk

Timeline for d1derg1:

• d1derg1 first appeared (with stable ids) in SCOP 1.55
  
• d1derg1 appears in SCOP 1.61
  
• d1derg1 does not appear in SCOP 1.65