SCOP 1.75: Domain d2ihva2: 2ihv A:12-197

Lineage for d2ihva2 (2ihv A:12-197)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology

6. Protein Carboxyethylarginine synthase [102330] (1 species)

7. Species Streptomyces clavuligerus [TaxId:1901] [102331] (6 PDB entries)

8. Domain d2ihva2: 2ihv A:12-197 [147701]
   Other proteins in same PDB: d2ihva1, d2ihva3, d2ihvb1, d2ihvb3, d2ihvd1, d2ihvd3
   automatically matched to d1upaa2
   complexed with gva, k, mg, tpp

Details for d2ihva2

PDB Entry: 2ihv, 2.3 Å

PDB Description: carboxyethylarginine synthase from streptomyces clavuligerus: 5- guanidinovaleric acid complex

PDB Compounds: (A:) carboxyethylarginine synthase

SCOP Domain Sequences for d2ihva2:

Sequence; same for both SEQRES and ATOM records:

>d2ihva2 c.36.1.5 (A:12-197) Carboxyethylarginine synthase {Streptomyces clavuligerus [TaxId: 1901]}
ptaahallsrlrdhgvgkvfgvvgreaasilfdevegidfvltrheftagvaadvlarit
grpqacwatlgpgmtnlstgiatsvldrspvialaaqseshdifpndthqcldsvaivap
mskyavelqrpheitdlvdsavnaamtepvgpsfislpvdllgssegidttvpnppantp
akpvgv

Timeline for d2ihva2:

• d2ihva2 is new in SCOP 1.75
  
• d2ihva2 appears in SCOPe 2.01
  
• d2ihva2 appears in the current release, SCOPe 2.08