Lineage for Protein: Peptidyl-prolyl cis-trans isomerase FkpA
- Root: SCOP 1.67
Class d: Alpha and beta proteins (a+b) [53931] (260 folds) 
Fold d.26: FKBP-like [54533] (3 superfamilies)
core: beta(2)-alpha-beta(2); antiparallel beta-sheet
Superfamily d.26.1: FKBP-like [54534] (3 families) 
Family d.26.1.1: FKBP immunophilin/proline isomerase [54535] (15 proteins) 
Protein Peptidyl-prolyl cis-trans isomerase FkpA [102866] (1 species)
similar to MIP; contains all-alpha dimerisation subdomain in the N-terminal extension
Species:
Escherichia coli [TaxId:562] [102867] (3 PDB entries) - Domains for 1q6h:
Domain d1q6ha_: 1q6h A: [95975] 
Domain d1q6hb_: 1q6h B: [95976]
- Domains for 1q6i:
Domain d1q6ia_: 1q6i A: [95977] 
Domain d1q6ib_: 1q6i B: [95978]
complexed with fk5
- Domain for 1q6u:
Domain d1q6ua_: 1q6u A: [95998]
complexed with cs
- Domains for 1q6h:
More info for Protein Peptidyl-prolyl cis-trans isomerase FkpA from d.26.1.1: FKBP immunophilin/proline isomerase
Timeline for Protein Peptidyl-prolyl cis-trans isomerase FkpA from d.26.1.1: FKBP immunophilin/proline isomerase:
- Protein Peptidyl-prolyl cis-trans isomerase FkpA from d.26.1.1: FKBP immunophilin/proline isomerase is new in SCOP 1.67
- Protein Peptidyl-prolyl cis-trans isomerase FkpA from d.26.1.1: FKBP immunophilin/proline isomerase appears in SCOP 1.69
- Protein Peptidyl-prolyl cis-trans isomerase FkpA from d.26.1.1: FKBP immunophilin/proline isomerase appears in the current release, SCOPe 2.08