SCOP 1.67: Domain d1h3da2: 1h3d A:225-299

Lineage for d1h3da2 (1h3d A:225-299)

1. Root: SCOP 1.67

2. Class d: Alpha and beta proteins (a+b) [53931] (260 folds)

3. Fold d.58: Ferredoxin-like [54861] (48 superfamilies)
   alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2

4. Superfamily d.58.5: GlnB-like [54913] (4 families)
   form timeric structures with the orthogonally packed beta-sheets

5. Family d.58.5.3: ATP phosphoribosyltransferase (ATP-PRTase, HisG), regulatory C-terminal domain [88851] (1 protein)

6. Protein ATP phosphoribosyltransferase (ATP-PRTase, HisG), regulatory C-terminal domain [82669] (2 species)
   binds allosteric inhibitor histidine

7. Species Escherichia coli [TaxId:562] [102977] (2 PDB entries)

8. Domain d1h3da2: 1h3d A:225-299 [90593]
   Other proteins in same PDB: d1h3da1
   complexed with amp, tla

Details for d1h3da2

PDB Entry: 1h3d, 2.7 Å

PDB Description: structure of the e.coli atp-phosphoribosyltransferase

SCOP Domain Sequences for d1h3da2:

Sequence, based on SEQRES records:

>d1h3da2 d.58.5.3 (A:225-299) ATP phosphoribosyltransferase (ATP-PRTase, HisG), regulatory C-terminal domain {Escherichia coli}
eskyimmhapterldeviallpgaerptilplagdqqrvamhmvssetlfwetmeklkal
gassilvlpiekmme

Sequence, based on observed residues (ATOM records):

>d1h3da2 d.58.5.3 (A:225-299) ATP phosphoribosyltransferase (ATP-PRTase, HisG), regulatory C-terminal domain {Escherichia coli}
eskyimmhapterldeviallpgaerptilplamhmvssetlfwetmeklkalgassilv
lpiekmme

Timeline for d1h3da2:

• d1h3da2 is new in SCOP 1.67
  
• d1h3da2 appears in SCOP 1.69
  
• d1h3da2 appears in the current release, SCOPe 2.08