Lineage for d1tiwa2 (1tiw A:262-610)

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 570217Fold c.1: TIM beta/alpha-barrel [51350] (32 superfamilies)
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. 574003Superfamily c.1.23: FAD-linked oxidoreductase [51730] (2 families) (S)
    distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation
  5. 574012Family c.1.23.2: Proline dehydrohenase domain of bifunctional PutA protein [82279] (1 protein)
  6. 574013Protein Proline dehydrohenase domain of bifunctional PutA protein [82280] (1 species)
  7. 574014Species Escherichia coli [TaxId:562] [82281] (5 PDB entries)
  8. 574017Domain d1tiwa2: 1tiw A:262-610 [112431]
    Other proteins in same PDB: d1tiwa1
    complexed with fad, tfb

Details for d1tiwa2

PDB Entry: 1tiw (more details), 2 Å

PDB Description: Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) complexed with L-Tetrahydro-2-furoic acid

SCOP Domain Sequences for d1tiwa2:

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

>d1tiwa2 c.1.23.2 (A:262-610) Proline dehydrohenase domain of bifunctional PutA protein {Escherichia coli}
getiaealanarkleekgfrysydmlgeaaltaadaqaymvsyqqaihaigkasngrgiy
egpgisiklsalhprysraqydrvmeelyprlksltllarqydiginidaeesdrleisl
dlleklcfepelagwngigfviqayqkrcplvidylidlatrsrrrlmirlvkgaywdse
ikraqmdglegypvytrkvytdvsylacakkllavpnliypqfathnahtlaaiyqlagq
nyypgqyefqclhgmgeplyeqvtgkvadgklnrpcriyapvgthetllaylvrrlleng
antsfvnriadtslpldelvadpvtaveklaqqegqtglphpkiplprd

SCOP Domain Coordinates for d1tiwa2:

Click to download the PDB-style file with coordinates for d1tiwa2.
(The format of our PDB-style files is described here.)

Timeline for d1tiwa2:

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Domains from same chain:
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d1tiwa1