SCOPe 2.06: Domain d2ck9e_: 2ck9 E:

Lineage for d2ck9e_ (2ck9 E:)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.2: Ribulose-phoshate binding barrel [51366] (7 families)

5. Family c.1.2.1: Histidine biosynthesis enzymes [51367] (3 proteins)
   structural evidence for the gene duplication within the barrel fold
   automatically mapped to Pfam PF00977

6. Protein Cyclase subunit (or domain) of imidazoleglycerolphosphate synthase HisF [51370] (4 species)

7. Species Thermotoga maritima [TaxId:2336] [51371] (5 PDB entries)

8. Domain d2ck9e_: 2ck9 E: [303668]
   Other proteins in same PDB: d2ck9b_, d2ck9d_, d2ck9f_
   automated match to d1gpwa_
   complexed with amz

Details for d2ck9e_

PDB Entry: 2ck9, 2.85 Å

PDB Description: structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex

PDB Compounds: (E:) Imidazole glycerol phosphate synthase subunit hisF

SCOPe Domain Sequences for d2ck9e_:

Sequence; same for both SEQRES and ATOM records:

>d2ck9e_ c.1.2.1 (E:) Cyclase subunit (or domain) of imidazoleglycerolphosphate synthase HisF {Thermotoga maritima [TaxId: 2336]}
mlakriiaclnvkdgrvvkgtnfenlrdsgdpvelgkfyseigidelvflditasvekrk
tmlelvekvaeqidipftvgggihdfetaselilrgadkvsintaavenpslitqiaqtf
gsqavvvaidakrvdgefmvftysgkkntgillrdwvvevekrgageilltsidrdgtks
gydtemirfvrplttlpiiasggagkmehfleaflagadaalaasvfhfreidvrelkey
lkkhgvnvrlegl

Timeline for d2ck9e_:

• d2ck9e_ is new in SCOPe 2.06-stable
  
• d2ck9e_ appears in SCOPe 2.07
  
• d2ck9e_ appears in the current release, SCOPe 2.08