SCOPe 2.07: Domain d2acua_: 2acu A:

Lineage for d2acua_ (2acu A:)

1. Root: SCOPe 2.07

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.7: NAD(P)-linked oxidoreductase [51430] (2 families)

5. Family c.1.7.1: Aldo-keto reductases (NADP) [51431] (16 proteins)
   Common fold covers whole protein structure

6. Protein Aldose reductase (aldehyde reductase) [51436] (2 species)

7. Species Human (Homo sapiens) [TaxId:9606] [51437] (155 PDB entries)
   Uniprot P15121

8. Domain d2acua_: 2acu A: [28676]
   complexed with cit, nap; mutant

Details for d2acua_

PDB Entry: 2acu, 1.76 Å

PDB Description: tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and the crystal structure of the y48h mutant enzyme

PDB Compounds: (A:) aldose reductase

SCOPe Domain Sequences for d2acua_:

Sequence; same for both SEQRES and ATOM records:

>d2acua_ c.1.7.1 (A:) Aldose reductase (aldehyde reductase) {Human (Homo sapiens) [TaxId: 9606]}
asrlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvhqnenevgvaiqe
klreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgke
ffpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpa
vnqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakh
nkttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvcal
lsctshkdypfheef

Timeline for d2acua_:

• d2acua_ first appeared (with stable ids) in SCOP 1.55, called d2acu__
  
• d2acua_ appears in SCOPe 2.06
  
• d2acua_ appears in the current release, SCOPe 2.08