SCOP 1.63: Domain d1l9mb4: 1l9m B:141-460

Lineage for d1l9mb4 (1l9m B:141-460)

1. Root: SCOP 1.63

2. Class d: Alpha and beta proteins (a+b) [53931] (224 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] (9 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 catalytic domain [54044] (1 protein)

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

7. Species Human (Homo sapiens), TGase E3 [TaxId:9606] [75334] (2 PDB entries)

8. Domain d1l9mb4: 1l9m B:141-460 [73739]
   Other proteins in same PDB: d1l9ma1, d1l9ma2, d1l9ma3, d1l9mb1, d1l9mb2, d1l9mb3
   complexed with br, ca, cl; mutant

Details for d1l9mb4

PDB Entry: 1l9m, 2.1 Å

PDB Description: three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

SCOP Domain Sequences for d1l9mb4:

Sequence; same for both SEQRES and ATOM records:

>d1l9mb4 d.3.1.4 (B:141-460) Transglutaminase catalytic domain {Human (Homo sapiens), TGase E3}
dsvfmgnhaereeyvqedagiifvgstnrigmigwnfgqfeedilsiclsildrslnfrr
daatdvasrndpkyvgrvlsaminsnddngvlagnwsgtytggrdprswdgsveilknwk
ksglspvrygqcwvfagtlntalrslgipsrvitnfnsahdtdrnlsvdvyydpmgnpld
kgsdsvwnfhvwnegwfvrsdlgpsyggwqvldatpqersqgvfqcgpasvigvregdvq
lnfdmpfifaevnadritwlydnttgkqwknsvnshtigryistkavgsnarmdvtdkyk
ypegsdqerqvfqkalgklk

Timeline for d1l9mb4:

• d1l9mb4 first appeared in SCOP 1.61
  
• d1l9mb4 appears in SCOP 1.65
  
• d1l9mb4 appears in the current release, SCOPe 2.08