SCOP 1.63: Domain d1mns_1: 1mns 133-359

Lineage for d1mns_1 (1mns 133-359)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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.1.11: Enolase C-terminal domain-like [51604] (2 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this family

5. Family c.1.11.2: D-glucarate dehydratase-like [51609] (7 proteins)

6. Protein Mandelate racemase [51617] (1 species)

7. Species Pseudomonas putida [TaxId:303] [51618] (6 PDB entries)

8. Domain d1mns_1: 1mns 133-359 [29246]
   Other proteins in same PDB: d1mns_2
   complexed with apg, mg

Details for d1mns_1

PDB Entry: 1mns, 2 Å

PDB Description: on the role of lysine 166 in the mechanism of mandelate racemase from pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (r)-alpha-phenylglycidate

SCOP Domain Sequences for d1mns_1:

Sequence; same for both SEQRES and ATOM records:

>d1mns_1 c.1.11.2 (133-359) Mandelate racemase {Pseudomonas putida}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv

Timeline for d1mns_1:

• d1mns_1 first appeared (with stable ids) in SCOP 1.55
  
• d1mns_1 appears in SCOP 1.61
  
• d1mns_1 appears in SCOP 1.65
  
• d1mns_1 appears in the current release, SCOPe 2.08, called d1mnsa1