Lineage for d2r5nb1 (2r5n B:333-527)

  1. Root: SCOP 1.75
  2. 814173Class c: Alpha and beta proteins (a/b) [51349] (147 folds)
  3. 828800Fold 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. 828801Superfamily 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. 828944Family c.36.1.6: TK-like Pyr module [88735] (2 proteins)
    different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain
  6. 828963Protein Transketolase (TK), Pyr module [88736] (4 species)
  7. 828979Species Escherichia coli [TaxId:562] [89650] (4 PDB entries)
  8. 828983Domain d2r5nb1: 2r5n B:333-527 [151594]
    Other proteins in same PDB: d2r5na2, d2r5na3, d2r5nb2, d2r5nb3
    automatically matched to d1qgda1
    complexed with ca, edo, r5p, rp5, tpp

Details for d2r5nb1

PDB Entry: 2r5n (more details), 1.6 Å

PDB Description: crystal structure of transketolase from escherichia coli in noncovalent complex with acceptor aldose ribose 5-phosphate
PDB Compounds: (B:) Transketolase 1

SCOP Domain Sequences for d2r5nb1:

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

>d2r5nb1 c.36.1.6 (B:333-527) Transketolase (TK), Pyr module {Escherichia coli [TaxId: 562]}
mpsdfdakakefiaklqanpakiasrkasqnaieafgpllpeflggsadlapsnltlwsg
skainedaagnyihygvrefgmtaiangislhggflpytstflmfveyarnavrmaalmk
qrqvmvythdsiglgedgpthqpveqvaslrvtpnmstwrpcdqvesavawkygverqdg
ptalilsrqnlaqqe

SCOP Domain Coordinates for d2r5nb1:

Click to download the PDB-style file with coordinates for d2r5nb1.
(The format of our PDB-style files is described here.)

Timeline for d2r5nb1: