SCOPe 2.01: Domain d2r9fa1: 2r9f A:33-354

Lineage for d2r9fa1 (2r9f A:33-354)

1. Root: SCOPe 2.01

2. Class d: Alpha and beta proteins (a+b) [53931] (376 folds)

3. Fold d.3: Cysteine proteinases [54000] (1 superfamily)
   consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn

4. Superfamily d.3.1: Cysteine proteinases [54001] (23 families)
   the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta-sheet

5. Family d.3.1.3: Calpain large subunit, catalytic domain (domain II) [54040] (1 protein)

6. Protein Calpain large subunit, catalytic domain (domain II) [54041] (5 species)
   includes the N-terminal 'sequence' domain I

7. Species Rat (Rattus norvegicus), mu-type [TaxId:10116] [75332] (10 PDB entries)
   Uniprot P97571 33-353

8. Domain d2r9fa1: 2r9f A:33-354 [151767]
   automatically matched to d1tloa_
   complexed with ca, cl, gol, k2z

Details for d2r9fa1

PDB Entry: 2r9f, 1.6 Å

PDB Description: calpain 1 proteolytic core inactivated by zlak-3002, an alpha- ketoamide

PDB Compounds: (A:) Calpain-1 catalytic subunit

SCOPe Domain Sequences for d2r9fa1:

Sequence; same for both SEQRES and ATOM records:

>d2r9fa1 d.3.1.3 (A:33-354) Calpain large subunit, catalytic domain (domain II) {Rat (Rattus norvegicus), mu-type [TaxId: 10116]}
naikylgqdyenlrarclqngvlfqddafppvshslgfkelgpnssktygikwkrptell
snpqfivdgatrtdicqgalgdcwllaaiasltlnetilhrvvpygqsfqegyagifhfq
lwqfgewvdvvvddllptkdgklvfvhsaqgnefwsallekayakvngsyealsggctse
afedftggvtewydlqkapsdlyqiilkalergsllgcsinisdirdleaitfknlvrgh
aysvtdakqvtyqgqrvnlirmrnpwgevewkgpwsdnsyewnkvdpyereqlrvkmedg
efwmsfrdfireftkleicnlt

Timeline for d2r9fa1:

• d2r9fa1 first appeared in SCOP 1.75
  
• d2r9fa1 appears in SCOPe 2.02
  
• d2r9fa1 appears in the current release, SCOPe 2.08, called d2r9fa_