SCOPe 2.08: Domain d1bzla1: 1bzl A:2-169,A:287-357

Lineage for d1bzla1 (1bzl A:2-169,A:287-357)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (25 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Trypanothione reductase, N- and C-terminal domain [418954] (3 species)

7. Species Trypanosoma cruzi [TaxId:5693] [419414] (4 PDB entries)

8. Domain d1bzla1: 1bzl A:2-169,A:287-357 [30521]
   Other proteins in same PDB: d1bzla2, d1bzla3, d1bzlb2, d1bzlb3
   complexed with fad, gcg
   has additional insertions and/or extensions that are not grouped together

Details for d1bzla1

PDB Entry: 1bzl, 2.4 Å

PDB Description: crystal structure of trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors

PDB Compounds: (A:) trypanothione reductase (oxidized form)

SCOPe Domain Sequences for d1bzla1:

Sequence; same for both SEQRES and ATOM records:

>d1bzla1 c.3.1.5 (A:2-169,A:287-357) Trypanothione reductase, N- and C-terminal domain {Trypanosoma cruzi [TaxId: 5693]}
mskifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpk
klmvtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegl
efflgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlql
qnagvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt

Timeline for d1bzla1:

• d1bzla1 first appeared (with stable ids) in SCOP 1.55
  
• d1bzla1 appears in SCOPe 2.07