Crystal Structure of Cell Binding Factor 2 from Helicobacter pylori in complex with I2CA
External Resource: Annotation
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
B | SurA_N_3 | e5ez1B2 | A: alpha arrays | X: Triger factor/SurA peptide-binding domain-like (From Homology) | H: Triger factor/SurA peptide-binding domain-like | T: Porin chaperone SurA, peptide-binding domain | F: SurA_N_3 | ECOD (1.6) |
B | Rotamase_3 | e5ez1B1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
A | SurA_N_3 | e5ez1A1 | A: alpha arrays | X: Triger factor/SurA peptide-binding domain-like (From Homology) | H: Triger factor/SurA peptide-binding domain-like | T: Porin chaperone SurA, peptide-binding domain | F: SurA_N_3 | ECOD (1.6) |
A | Rotamase_3 | e5ez1A2 | 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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| Putative peptidyl-prolyl cis-trans isomerase HP_0175 | | - | - |