SCOPe 2.05: Domain d1raka1: 1rak A:4-55,A:376-426

Lineage for d1raka1 (1rak A:4-55,A:376-426)

1. Root: SCOPe 2.05

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 d1raka1: 1rak A:4-55,A:376-426 [111761]
   Other proteins in same PDB: d1raka2
   complexed with fe, fpy, gol; mutant

Details for d1raka1

PDB Entry: 1rak, 1.32 Å

PDB Description: bacterial cytosine deaminase d314s mutant bound to 5-fluoro-4-(s)- hydroxyl-3,4-dihydropyrimidine.

PDB Compounds: (A:) Cytosine deaminase

SCOPe Domain Sequences for d1raka1:

Sequence; same for both SEQRES and ATOM records:

>d1raka1 b.92.1.2 (A:4-55,A:376-426) Cytosine deaminase {Escherichia coli [TaxId: 562]}
alqtiinarlpgeeglwqihlqdgkisaidaqsgvmpitensldaeqglvipXliilpae
ngfdalrrqvpvrysvrggkviastqpaqttvyleqpeaidykr

Timeline for d1raka1:

• d1raka1 first appeared in SCOP 1.71
  
• d1raka1 appears in SCOPe 2.04
  
• d1raka1 appears in SCOPe 2.06
  
• d1raka1 appears in the current release, SCOPe 2.08