SCOPe 2.06: Domain d2mnra1: 2mnr A:133-359

Lineage for d2mnra1 (2mnr A:133-359)

1. Root: SCOPe 2.06

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.1.11: Enolase C-terminal domain-like [51604] (3 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this superfamily

5. Family c.1.11.2: D-glucarate dehydratase-like [51609] (15 proteins)

6. Protein Mandelate racemase [51617] (3 species)

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

8. Domain d2mnra1: 2mnr A:133-359 [29245]
   Other proteins in same PDB: d2mnra2
   complexed with mn, so4

Details for d2mnra1

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

PDB Compounds: (A:) mandelate racemase

SCOPe Domain Sequences for d2mnra1:

Sequence; same for both SEQRES and ATOM records:

>d2mnra1 c.1.11.2 (A:133-359) Mandelate racemase {Pseudomonas putida [TaxId: 303]}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv

Timeline for d2mnra1:

• d2mnra1 first appeared (with stable ids) in SCOP 1.55, called d2mnr_1
  
• d2mnra1 appears in SCOPe 2.05
  
• d2mnra1 appears in SCOPe 2.07
  
• d2mnra1 appears in the current release, SCOPe 2.08