SCOPe 2.06: Domain d1zczb2: 1zcz B:158-452

Lineage for d1zczb2 (1zcz B:158-452)

1. Root: SCOPe 2.06

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

3. Fold c.97: Cytidine deaminase-like [53926] (2 superfamilies)
   core: alpha-beta(2)-(alpha-beta)2; 3 layers (a/b/a); mixed beta-sheet of 4 strands, order 2134; strand 1 is antiparallel to the rest

4. Superfamily c.97.1: Cytidine deaminase-like [53927] (7 families)
   contains extra C-terminal strand 5, order 21345

5. Family c.97.1.4: AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC [64198] (1 protein)
   duplication: consists of two domains of this fold with extra secondary structures within and in between the two core motifs

6. Protein AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC [64199] (3 species)

7. Species Thermotoga maritima [TaxId:2336] [142844] (1 PDB entry)
   Uniprot Q9X0X6 158-452

8. Domain d1zczb2: 1zcz B:158-452 [124926]
   Other proteins in same PDB: d1zcza1, d1zczb1, d1zczb3
   automated match to d1zcza2
   complexed with k, pg4

Details for d1zczb2

PDB Entry: 1zcz, 1.88 Å

PDB Description: crystal structure of phosphoribosylaminoimidazolecarboxamide formyltransferase / imp cyclohydrolase (tm1249) from thermotoga maritima at 1.88 a resolution

PDB Compounds: (B:) Bifunctional purine biosynthesis protein PURH

SCOPe Domain Sequences for d1zczb2:

Sequence; same for both SEQRES and ATOM records:

>d1zczb2 c.97.1.4 (B:158-452) AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC {Thermotoga maritima [TaxId: 2336]}
islafkredlqlrygenphekafvygkpafeilhegktisfnnildaenawfmaknlprm
gavvvkhqspcgaaigedkveivkkaieaddessfggilavnfemdeevakslkkylevi
vapsftqeaievlskkkvrllkpgdyaswagkmafgslvlserkypegnfelvvgeplse
keledlefayrvvegaksnavliakdgvtvgigsgqpsrkraawiatvmagekakgavaa
sdaffpfpdsleilaqagvkavvaplgsirdeeviekarelgitfykapsrvfrh

Timeline for d1zczb2:

• d1zczb2 first appeared in SCOP 1.73
  
• d1zczb2 appears in SCOPe 2.05
  
• d1zczb2 appears in SCOPe 2.07
  
• d1zczb2 appears in the current release, SCOPe 2.08