SCOP 1.63: Domain d1o99a1: 1o99 A:77-310

Lineage for d1o99a1 (1o99 A:77-310)

1. Root: SCOP 1.63

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

3. Fold c.105: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain [64157] (1 superfamily)
   core:3 layers: a/b/a; mixed beta-sheet of 8 strands, order 45321678, strands 4 and 5 are antiparallel to the rest

4. Superfamily c.105.1: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain [64158] (1 family)

5. Family c.105.1.1: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain [64159] (1 protein)

6. Protein 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain [64160] (1 species)

7. Species Bacillus stearothermophilus [TaxId:1422] [64161] (3 PDB entries)

8. Domain d1o99a1: 1o99 A:77-310 [81235]
   Other proteins in same PDB: d1o99a2
   complexed with 2pg, mn, so4; mutant

Details for d1o99a1

PDB Entry: 1o99, 2.65 Å

PDB Description: crystal structure of the s62a mutant of phosphoglycerate mutase from bacillus stearothermophilus complexed with 2-phosphoglycerate

SCOP Domain Sequences for d1o99a1:

Sequence; same for both SEQRES and ATOM records:

>d1o99a1 c.105.1.1 (A:77-310) 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain {Bacillus stearothermophilus}
qsltriniairegefdrnetflaamnhvkqhgtslhlfgllsdggvhshihhlyallrla
akegvkrvyihgfldgrdvgpqtapqyikelqekikeygvgeiatlsgryysmdrdkrwd
rvekayramvygegptyrdpleciedsykhgiydefvlpsvivredgrpvatiqdndaii
fynfrpdraiqisntftnedfrefdrgpkhpkhlffvclthfsetvagyvafkp

Timeline for d1o99a1:

• d1o99a1 is new in SCOP 1.63
  
• d1o99a1 appears in SCOP 1.65
  
• d1o99a1 appears in the current release, SCOPe 2.08