SCOPe 2.08: Domain d1r1ra2: 1r1r A:222-737

Lineage for d1r1ra2 (1r1r A:222-737)

1. Root: SCOPe 2.08

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

3. Fold c.7: PFL-like glycyl radical enzymes [51997] (1 superfamily)
   contains: barrel, closed; n=10, S=10; accommodates a hairpin loop inside the barrel

4. Superfamily c.7.1: PFL-like glycyl radical enzymes [51998] (6 families)
   duplication: the N- and C-terminal halves have similar topologies

5. Family c.7.1.2: R1 subunit of ribonucleotide reductase, C-terminal domain [52002] (1 protein)
   automatically mapped to Pfam PF02867

6. Protein R1 subunit of ribonucleotide reductase, C-terminal domain [52003] (2 species)

7. Species Escherichia coli [TaxId:562] [52004] (10 PDB entries)

8. Domain d1r1ra2: 1r1r A:222-737 [30680]
   Other proteins in same PDB: d1r1ra1, d1r1rb1, d1r1rc1
   mutant

Details for d1r1ra2

PDB Entry: 1r1r, 2.9 Å

PDB Description: ribonucleotide reductase r1 protein mutant y730f with a reduced active site from escherichia coli

PDB Compounds: (A:) ribonucleotide reductase r1 protein

SCOPe Domain Sequences for d1r1ra2:

Sequence; same for both SEQRES and ATOM records:

>d1r1ra2 c.7.1.2 (A:222-737) R1 subunit of ribonucleotide reductase, C-terminal domain {Escherichia coli [TaxId: 562]}
fsscvliecgdsldsinatssaivkyvsqragiginagriralgspirggeafhtgcipf
ykhfqtavkscsqggvrggaatlfypmwhlevesllvlknnrgvegnrvrhmdygvqink
lmytrllkgeditlfspsdvpglydaffadqeeferlytkyekddsirkqrvkavelfsl
mmqerastgriyiqnvdhcnthspfdpaiapvrqsnlcleialptkplndvndengeial
ctlsafnlgainnldeleelailavraldalldyqdypipaakrgamgrrtlgigvinfa
yylakhgkrysdgsannlthktfeaiqyyllkasnelakeqgacpwfnettyakgilpid
tykkdldtianeplhydwealresikthglrnstlsalmpsetssqisnatngiepprgy
vsikaskdgilrqvvpdyehlhdayellwempgndgylqlvgimqkfidqsisantnydp
srfpsgkvpmqqllkdlltaykfgvktlfyqntrdg

Timeline for d1r1ra2:

• d1r1ra2 first appeared (with stable ids) in SCOP 1.55
  
• d1r1ra2 appears in SCOPe 2.07