Lineage for d1l9na4 (1l9n A:141-460)

  1. Root: SCOPe 2.01
  2. 1013083Class d: Alpha and beta proteins (a+b) [53931] (376 folds)
  3. 1014844Fold 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. 1014845Superfamily d.3.1: Cysteine proteinases [54001] (23 families) (S)
    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. 1015240Family d.3.1.4: Transglutaminase core [54044] (3 proteins)
  6. 1015246Protein Transglutaminase catalytic domain [54045] (4 species)
  7. 1015264Species Human (Homo sapiens), TGase E3 [TaxId:9606] [75334] (5 PDB entries)
  8. 1015265Domain d1l9na4: 1l9n A:141-460 [73743]
    Other proteins in same PDB: d1l9na1, d1l9na2, d1l9na3, d1l9nb1, d1l9nb2, d1l9nb3
    complexed with bgl, ca, cl

Details for d1l9na4

PDB Entry: 1l9n (more details), 2.1 Å

PDB Description: three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
PDB Compounds: (A:) Protein-glutamine glutamyltransferase E3

SCOPe Domain Sequences for d1l9na4:

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

>d1l9na4 d.3.1.4 (A:141-460) Transglutaminase catalytic domain {Human (Homo sapiens), TGase E3 [TaxId: 9606]}
dsvfmgnhaereeyvqedagiifvgstnrigmigwnfgqfeedilsiclsildrslnfrr
daatdvasrndpkyvgrvlsaminsnddngvlagnwsgtytggrdprswdgsveilknwk
ksglspvrygqcwvfagtlntalrslgipsrvitnfnsahdtdrnlsvdvyydpmgnpld
kgsdsvwnfhvwnegwfvrsdlgpsyggwqvldatpqersqgvfqcgpasvigvregdvq
lnfdmpfifaevnadritwlydnttgkqwknsvnshtigryistkavgsnarmdvtdkyk
ypegsdqerqvfqkalgklk

SCOPe Domain Coordinates for d1l9na4:

Click to download the PDB-style file with coordinates for d1l9na4.
(The format of our PDB-style files is described here.)

Timeline for d1l9na4: