SCOPe 2.08: Domain d2fymf1: 2fym F:140-431

Lineage for d2fymf1 (2fym F:140-431)

1. Root: SCOPe 2.08

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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.1.11: Enolase C-terminal domain-like [51604] (3 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this superfamily

5. Family c.1.11.1: Enolase [51605] (2 proteins)
   automatically mapped to Pfam PF00113

6. Protein Enolase [51606] (11 species)
   Fold of this protein slightly differs from common fold in topology

7. Species Escherichia coli [TaxId:562] [69396] (3 PDB entries)

8. Domain d2fymf1: 2fym F:140-431 [134385]
   Other proteins in same PDB: d2fyma2, d2fymc2, d2fymd2, d2fymf2
   automatically matched to d1e9id1
   protein/RNA complex; complexed with mg

Details for d2fymf1

PDB Entry: 2fym, 1.6 Å

PDB Description: crystal structure of e. coli enolase complexed with the minimal binding segment of rnase e.

PDB Compounds: (F:) enolase

SCOPe Domain Sequences for d2fymf1:

Sequence; same for both SEQRES and ATOM records:

>d2fymf1 c.1.11.1 (F:140-431) Enolase {Escherichia coli [TaxId: 562]}
pgkysmpvpmmniinggehadnnvdiqefmiqpvgaktvkeairmgsevfhhlakvlkak
gmntavgdeggyapnlgsnaealaviaeavkaagyelgkditlamdcaasefykdgkyvl
agegnkaftseefthfleeltkqypivsiedgldesdwdgfayqtkvlgdkiqlvgddlf
vtntkilkegiekgiansilikfnqigsltetlaaikmakdagytavishrsgetedati
adlavgtaagqiktgsmsrsdrvakynqlirieealgekapyngrkeikgqa

Timeline for d2fymf1:

• d2fymf1 first appeared in SCOP 1.73
  
• d2fymf1 appears in SCOPe 2.07