SCOPe 2.06: Domain d1l9na4: 1l9n A:141-460

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

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 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] (24 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.3.1.4: Transglutaminase core [54044] (3 proteins)

6. Protein Transglutaminase catalytic domain [54045] (4 species)

7. Species Human (Homo sapiens), TGase E3 [TaxId:9606] [75334] (9 PDB entries)

8. Domain 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, 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:

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

Timeline for d1l9na4:

• d1l9na4 first appeared in SCOP 1.61
  
• d1l9na4 appears in SCOPe 2.05
  
• d1l9na4 appears in SCOPe 2.07
  
• d1l9na4 appears in the current release, SCOPe 2.08