SCOP 1.65: Domain d1ni4b1: 1ni4 B:0-191

Lineage for d1ni4b1 (1ni4 B:0-191)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. Fold 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. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families)
   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. Family c.36.1.7: Branched-chain alpha-keto acid dehydrogenase Pyr module [88741] (4 proteins)
   parent family to TK and PFOR
   heterodimeric protein related to TK; alpha-subunit is the PP module and the N-terminal domain of beta-subunit is the Pyr module

6. Protein E1-beta subunit of pyruvate dehydrogenase, Pyr module [69472] (2 species)
   structure determined on its own rather in the complex with E1-alpha

7. Species Human (Homo sapiens) [TaxId:9606] [89653] (1 PDB entry)

8. Domain d1ni4b1: 1ni4 B:0-191 [85729]
   Other proteins in same PDB: d1ni4a_, d1ni4b2, d1ni4c_, d1ni4d2

Details for d1ni4b1

PDB Entry: 1ni4, 1.95 Å

PDB Description: human pyruvate dehydrogenase

SCOP Domain Sequences for d1ni4b1:

Sequence; same for both SEQRES and ATOM records:

>d1ni4b1 c.36.1.7 (B:0-191) E1-beta subunit of pyruvate dehydrogenase, Pyr module {Human (Homo sapiens)}
slqvtvrdainqgmdeelerdekvfllgeevaqydgaykvsrglwkkygdkriidtpise
mgfagiavgaamaglrpicefmtfnfsmqaidqvinsaaktyymsgglqpvpivfrgpng
asagvaaqhsqcfaawyghcpglkvvspwnsedakgliksairdnnpvvvlenelmygvp
fefppeaqskdf

Timeline for d1ni4b1:

• d1ni4b1 is new in SCOP 1.65
  
• d1ni4b1 appears in SCOP 1.67
  
• d1ni4b1 appears in the current release, SCOPe 2.08