SCOPe 2.08: Domain d1ekva_: 1ekv A:

Lineage for d1ekva_ (1ekv A:)

1. Root: SCOPe 2.08

2. Class e: Multi-domain proteins (alpha and beta) [56572] (74 folds)

3. Fold e.17: D-aminoacid aminotransferase-like PLP-dependent enzymes [56751] (1 superfamily)
   2 domains: (1) alpha+beta: beta3-alpha2-beta2; (2) alpha/beta, a part of its mixed sheet forms barrel: n=6, S=8

4. Superfamily e.17.1: D-aminoacid aminotransferase-like PLP-dependent enzymes [56752] (2 families)

5. Family e.17.1.1: D-aminoacid aminotransferase-like PLP-dependent enzymes [56753] (4 proteins)

6. Protein Branched-chain aminoacid aminotransferase [56757] (2 species)

7. Species Human (Homo sapiens), mitochondrial [TaxId:9606] [64508] (26 PDB entries)

8. Domain d1ekva_: 1ekv A: [59449]
   complexed with plp, trs

Details for d1ekva_

PDB Entry: 1ekv, 2.25 Å

PDB Description: human branched chain amino acid aminotransferase (mitochondrial): three dimensional structure of enzyme inactivated by tris bound to the pyridoxal-5'-phosphate on one end and active site lys202 nz on the other.

PDB Compounds: (A:) branched chain amino acid aminotransferase (mitochondrial)

SCOPe Domain Sequences for d1ekva_:

Sequence; same for both SEQRES and ATOM records:

>d1ekva_ e.17.1.1 (A:) Branched-chain aminoacid aminotransferase {Human (Homo sapiens), mitochondrial [TaxId: 9606]}
asssfkaadlqlemtqkphkkpgpgeplvfgktftdhmlmvewndkgwgqpriqpfqnlt
lhpassslhyslqlfegmkafkgkdqqvrlfrpwlnmdrmlrsamrlclpsfdklellec
irrlievdkdwvpdaagtslyvrpvlignepslgvsqprrallfvilcpvgayfpggsvt
pvslladpafirawvggvgnyklggnygptvlvqqealkrgceqvlwlygpdhqltevgt
mnifvywthedgvlelvtpplngvilpgvvrqslldmaqtwgefrvvertitmkqllral
eegrvrevfgsgtacqvcpvhrilykdrnlhiptmengpelilrfqkelkeiqygirahe
wmfpv

Timeline for d1ekva_:

• d1ekva_ first appeared in SCOP 1.57
  
• d1ekva_ appears in SCOPe 2.07