Structural Classification of Proteins and ASTRAL release 1.75 (June 2009)
Search SCOP (example):

Lineage for d1efva2 (1efv A:208-331)

  1. Root: SCOP 1.75
  2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)
  3. Fold c.31: DHS-like NAD/FAD-binding domain [52466] (1 superfamily)
    3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like
  4. Superfamily c.31.1: DHS-like NAD/FAD-binding domain [52467] (6 families) (S)
    binds cofactor molecules in the opposite direction than classical Rossmann fold
  5. Family c.31.1.2: C-terminal domain of the electron transfer flavoprotein alpha subunit [52471] (1 protein)
    lacks strand 3; shares the FAD-binding mode with the pyruvate oxidase domain
  6. Protein C-terminal domain of the electron transfer flavoprotein alpha subunit [52472] (3 species)
  7. Species Human (Homo sapiens) [TaxId:9606] [52473] (3 PDB entries)
  8. Domain d1efva2: 1efv A:208-331 [31728]
    Other proteins in same PDB: d1efva1, d1efvb_
    complexed with amp, fad

Details for d1efva2

PDB Entry: 1efv (more details)
PDB Description: three-dimensional structure of human electron transfer flavoprotein to 2.1 a resolution
PDB Compounds: (A:) electron transfer flavoprotein

SCOP Domain Sequences for d1efva2:

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

>d1efva2 c.31.1.2 (A:208-331) C-terminal domain of the electron transfer flavoprotein alpha subunit {Human (Homo sapiens) [TaxId: 9606]}
drpeltgakvvvsggrglksgenfkllydladqlhaavgasraavdagfvpndmqvgqtg
kivapelyiavgisgaiqhlagmkdsktivainkdpeapifqvadygivadlfkvvpemt
eilk

SCOP Domain Coordinates for d1efva2:

Click to download the PDB-style file with coordinates for d1efva2.
(The format of our PDB-style files is described here.)

Timeline for d1efva2:

d1efva2 appears in SCOP 1.73
d1efva2 appears in SCOP 1.75A


d1efva2
(click for larger image)


d1efva2 in context of chain
Domains from same chain:
d1efva1


d1efva2 in context of PDB
Domains from other chains:
d1efvb_


SCOP Copyright © 1994-2013 The SCOP and Astral authors
scop@mrc-lmb.cam.ac.uk and astral@compbio.berkeley.edu