SCOPe 2.04: Domain d1ra0a1: 1ra0 A:4-55,A:376-426

Lineage for d1ra0a1 (1ra0 A:4-55,A:376-426)

1. Root: SCOPe 2.04

2. Class b: All beta proteins [48724] (176 folds)

3. Fold b.92: Composite domain of metallo-dependent hydrolases [51337] (1 superfamily)
   pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns

4. Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (12 families)
   this domain is interrupted by the catalytic beta/alpha barrel domain

5. Family b.92.1.2: Cytosine deaminase [69373] (1 protein)

6. Protein Cytosine deaminase [69374] (1 species)

7. Species Escherichia coli [TaxId:562] [69375] (8 PDB entries)
   Uniprot P25524

8. Domain d1ra0a1: 1ra0 A:4-55,A:376-426 [111756]
   Other proteins in same PDB: d1ra0a2
   complexed with fe, fpy; mutant

Details for d1ra0a1

PDB Entry: 1ra0, 1.12 Å

PDB Description: bacterial cytosine deaminase d314g mutant bound to 5-fluoro-4-(s)- hydroxy-3,4-dihydropyrimidine.

PDB Compounds: (A:) Cytosine deaminase

SCOPe Domain Sequences for d1ra0a1:

Sequence; same for both SEQRES and ATOM records:

>d1ra0a1 b.92.1.2 (A:4-55,A:376-426) Cytosine deaminase {Escherichia coli [TaxId: 562]}
alqtiinarlpgeeglwqihlqdgkisaidaqsgvmpitensldaeqglvipXliilpae
ngfdalrrqvpvrysvrggkviastqpaqttvyleqpeaidykr

Timeline for d1ra0a1:

• d1ra0a1 first appeared in SCOP 1.71
  
• d1ra0a1 appears in SCOPe 2.03
  
• d1ra0a1 appears in SCOPe 2.05
  
• d1ra0a1 appears in the current release, SCOPe 2.08