SCOP 1.65: Domain d2mnr_1: 2mnr 133-359

Lineage for d2mnr_1 (2mnr 133-359)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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 d2mnr_1: 2mnr 133-359 [29245]
   Other proteins in same PDB: d2mnr_2
   complexed with mn, so4

Details for d2mnr_1

PDB Entry: 2mnr, 1.9 Å

PDB Description: mechanism of the reaction catalyzed by mandelate racemase. 2. crystal structure of mandelate racemase at 2.5 angstroms resolution: identification of the active site and possible catalytic residues

SCOP Domain Sequences for d2mnr_1:

Sequence; same for both SEQRES and ATOM records:

>d2mnr_1 c.1.11.2 (133-359) Mandelate racemase {Pseudomonas putida}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv

Timeline for d2mnr_1:

• d2mnr_1 first appeared (with stable ids) in SCOP 1.55
  
• d2mnr_1 appears in SCOP 1.63
  
• d2mnr_1 appears in SCOP 1.67
  
• d2mnr_1 appears in the current release, SCOPe 2.08, called d2mnra1