Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1nmwa_ Alpha and beta proteins (a+b) FKBP-like FKBP-like FKBP immunophilin/proline isomerase Mitotic rotamase PIN1, domain 2 human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyRotamase-like8036947 3000622 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ARotamase_3e1nmwA1 A: a+b two layersX: FKBP-likeH: FKBP-likeT: FKBP-likeF: Rotamase_3ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.10.50.40 Alpha Beta Roll Chitinase A domain 3CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00639PPIC-type PPIASE domain (Rotamase)PPIC-type PPIASE domainRotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
peptidylprolyl isomerase (PpiC-type)  M-CSA #511

Prolyl isomerase is able to convert the cis and trans forms of peptide bonds involving proline. This alters the 3d structure of the target proteins, which activates them or deactivates them so that they can take part in signal pathways inside the cell. The human prolyl isomerase hPin1 targets many important proteins after they have been phosphorylated by ser/thr kinases, being involved specifically in G2/M transitions in the cell cycle. As a result, mutations to the protein have been implicated in many forms of cancer.

Defined by 5 residues: HIS:A-10 [auth A-59]CYS:A-64 [auth A-113]GLN:A-82 [auth A-131]SER:A-105 [auth A-154]HIS:A-108 [auth A-157]
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