Lineage for d1ekvb_ (1ekv B:)

  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) (S)
  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 d1ekvb_: 1ekv B: [59450]
    complexed with plp, trs

Details for d1ekvb_

PDB Entry: 1ekv (more details), 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: (B:) branched chain amino acid aminotransferase (mitochondrial)

SCOPe Domain Sequences for d1ekvb_:

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

>d1ekvb_ e.17.1.1 (B:) Branched-chain aminoacid aminotransferase {Human (Homo sapiens), mitochondrial [TaxId: 9606]}
asssfkaadlqlemtqkphkkpgpgeplvfgktftdhmlmvewndkgwgqpriqpfqnlt
lhpassslhyslqlfegmkafkgkdqqvrlfrpwlnmdrmlrsamrlclpsfdklellec
irrlievdkdwvpdaagtslyvrpvlignepslgvsqprrallfvilcpvgayfpggsvt
pvslladpafirawvggvgnyklggnygptvlvqqealkrgceqvlwlygpdhqltevgt
mnifvywthedgvlelvtpplngvilpgvvrqslldmaqtwgefrvvertitmkqllral
eegrvrevfgsgtacqvcpvhrilykdrnlhiptmengpelilrfqkelkeiqygirahe
wmfpv

SCOPe Domain Coordinates for d1ekvb_ are not available.

Timeline for d1ekvb_:

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Domains from other chains:
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d1ekva_