Lineage for d3reqb2 (3req B:476-637)

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2101600Fold c.23: Flavodoxin-like [52171] (15 superfamilies)
    3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345
  4. 2102924Superfamily c.23.6: Cobalamin (vitamin B12)-binding domain [52242] (1 family) (S)
  5. 2102925Family c.23.6.1: Cobalamin (vitamin B12)-binding domain [52243] (5 protein domains)
  6. 2102967Protein Methylmalonyl-CoA mutase beta subunit, C-terminal domain [88719] (1 species)
    inactive subunit
  7. 2102968Species Propionibacterium freudenreichii, subsp. shermanii [TaxId:1744] [88720] (8 PDB entries)
  8. 2102983Domain d3reqb2: 3req B:476-637 [31272]
    Other proteins in same PDB: d3reqa1, d3reqa2, d3reqb1
    complexed with adn, b12

Details for d3reqb2

PDB Entry: 3req (more details), 2.7 Å

PDB Description: methylmalonyl-coa mutase, substrate-free state (poor quality structure)
PDB Compounds: (B:) methylmalonyl-coa mutase

SCOPe Domain Sequences for d3reqb2:

Sequence, based on SEQRES records: (download)

>d3reqb2 c.23.6.1 (B:476-637) Methylmalonyl-CoA mutase beta subunit, C-terminal domain {Propionibacterium freudenreichii, subsp. shermanii [TaxId: 1744]}
tkpfpaaparkglawhrdsevfeqlmdrstsvserpkvflaclgtrrdfggregfsspvw
hiagidtpqveggttaeiveafkksgaqvadlcssakvyaqqglevakalkaagakalyl
sgafkefgddaaeaeklidgrlfmgmdvvdtlsstldilgva

Sequence, based on observed residues (ATOM records): (download)

>d3reqb2 c.23.6.1 (B:476-637) Methylmalonyl-CoA mutase beta subunit, C-terminal domain {Propionibacterium freudenreichii, subsp. shermanii [TaxId: 1744]}
tkpfpaaparkglawhrdsevfeqlmdrstsvserpkvflaclgtrrdfggregfsspvw
hiagidtpqvettaeiveafkksgaqvadlcssakvyaqqglevakalkaagakalylsg
afkefgddaaeaeklidgrlfmgmdvvdtlsstldilgva

SCOPe Domain Coordinates for d3reqb2:

Click to download the PDB-style file with coordinates for d3reqb2.
(The format of our PDB-style files is described here.)

Timeline for d3reqb2:

View in 3D
Domains from same chain:
(mouse over for more information)
d3reqb1