7F0M
Crystal Structure of human Pin1 complexed with a potent covalent inhibitor
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
B | SCOP2B Superfamily | Rotamase-like | 8036947 | 3000622 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Rotamase-like | 8036947 | 3000622 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Rotamase-like | 8036947 | 3000622 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Rotamase-like | 8036947 | 3000622 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | WW | e7f0mB2 | A: beta meanders | X: WW domain-like | H: WW domain (From Topology) | T: WW domain | F: WW | ECOD (1.6) |
B | Rotamase_3 | e7f0mB1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
D | WW | e7f0mD2 | A: beta meanders | X: WW domain-like | H: WW domain (From Topology) | T: WW domain | F: WW | ECOD (1.6) |
D | Rotamase_3 | e7f0mD1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
A | WW | e7f0mA2 | A: beta meanders | X: WW domain-like | H: WW domain (From Topology) | T: WW domain | F: WW | ECOD (1.6) |
A | Rotamase_3 | e7f0mA1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
C | WW | e7f0mC2 | A: beta meanders | X: WW domain-like | H: WW domain (From Topology) | T: WW domain | F: WW | ECOD (1.6) |
C | Rotamase_3 | e7f0mC1 | A: a+b two layers | X: FKBP-like | H: FKBP-like | T: FKBP-like | F: Rotamase_3 | ECOD (1.6) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
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 | |
PF00397 | WW domain (WW) | WW domain | The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR036020 | WW domain superfamily | Homologous Superfamily | |
IPR023058 | Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site | Conserved Site | |
IPR046357 | Peptidyl-prolyl cis-trans isomerase domain superfamily | Homologous Superfamily | |
IPR000297 | Peptidyl-prolyl cis-trans isomerase, PpiC-type | Domain | |
IPR051370 | Peptidyl-prolyl cis-trans isomerase Pin1 | Family | |
IPR001202 | WW domain | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Chains | Drug Target   | Associated Disease |
---|---|---|
Q13526 | :