Solution structure of Pin1At from Arabidopsis thaliana
External Resource: Annotation
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
A | SCOP2 Family | FKBP immunophilin/proline isomerase | 8027486 | 4001062 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | Rotamase-like | 8039865 | 3000622 | SCOP2 (2022-06-29) |
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
A | Rotamase_3 | e1j6yA1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
Chains | Accession | Name | Description | Comments | Source |
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| PF00639 | PPIC-type PPIASE domain (Rotamase) | PPIC-type PPIASE domain | Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. | Domain |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| peptidyl-prolyl cis-trans isomerase | | | |