SCOP 1.75: Domain d1sgxa4: 1sgx A:141-461

Lineage for d1sgxa4 (1sgx A:141-461)

1. Root: SCOP 1.75

2. Class d: Alpha and beta proteins (a+b) [53931] (376 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] (22 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] (2 proteins)

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

7. Species Human (Homo sapiens), TGase E3 [TaxId:9606] [75334] (8 PDB entries)

8. Domain d1sgxa4: 1sgx A:141-461 [98865]
   Other proteins in same PDB: d1sgxa1, d1sgxa2, d1sgxa3, d1sgxb1, d1sgxb2, d1sgxb3

Details for d1sgxa4

PDB Entry: 1sgx, 2 Å

PDB Description: Crystal Structure of Transglutaminase 3 in Complex with Bound GMP: Structural Basis for Alteration in Nucleotide Specificity

PDB Compounds: (A:) Protein-glutamine glutamyltransferase E

SCOP Domain Sequences for d1sgxa4:

Sequence; same for both SEQRES and ATOM records:

>d1sgxa4 d.3.1.4 (A:141-461) Transglutaminase catalytic domain {Human (Homo sapiens), TGase E3 [TaxId: 9606]}
dsvfmgnhaereeyvqedagiifvgstnrigmigwnfgqfeedilsiclsildrslnfrr
daatdvasrndpkyvgrvlsaminsnddngvlagnwsgtytggrdprswngsveilknwk
ksglspvrygqcwvfagtlntalrslgipsrvitnfnsahdtdrnlsvdvyydpmgnpld
kgsdsvwnfhvwnegwfvrsdlgpsyggwqvldatpqersqgvfqcgpasvigvregdvq
lnfdmpfifaevnadritwlydnttgkqwknsvnshtigryistkavgsnarmdvtdkyk
ypegsdqerqvfqkalgklkp

Timeline for d1sgxa4:

• d1sgxa4 first appeared in SCOP 1.67
  
• d1sgxa4 appears in SCOP 1.73
  
• d1sgxa4 does not appear in SCOPe 2.01