Lineage for d1ovmc3 (1ovm C:356-551)

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 581036Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
    3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465
  4. 581037Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families) (S)
    there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
    two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules
  5. 581216Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (7 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
  6. 581281Protein Indole-3-pyruvate decarboxylase [89654] (1 species)
  7. 581282Species Enterobacter cloacae [TaxId:550] [89655] (1 PDB entry)
  8. 581285Domain d1ovmc3: 1ovm C:356-551 [87469]
    Other proteins in same PDB: d1ovma1, d1ovma2, d1ovmb1, d1ovmb2, d1ovmc1, d1ovmc2, d1ovmd1, d1ovmd2

Details for d1ovmc3

PDB Entry: 1ovm (more details), 2.65 Å

PDB Description: Crystal structure of Indolepyruvate decarboxylase from Enterobacter cloacae

SCOP Domain Sequences for d1ovmc3:

Sequence; same for both SEQRES and ATOM records: (download)

>d1ovmc3 c.36.1.9 (C:356-551) Indole-3-pyruvate decarboxylase {Enterobacter cloacae}
pdgsltqenfwrtlqtfirpgdiiladqgtsafgaidlrlpadvnfivqplwgsigytla
aafgaqtacpnrrvivltgdgaaqltiqelgsmlrdkqhpiilvlnnegytveraihgae
qryndialwnwthipqalsldpqsecwrvseaeqladvlekvahherlslievmlpkadi
ppllgaltkaleacnn

SCOP Domain Coordinates for d1ovmc3:

Click to download the PDB-style file with coordinates for d1ovmc3.
(The format of our PDB-style files is described here.)

Timeline for d1ovmc3: