Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth B]SCOP2B SuperfamilyLeucine zipper-like8037025 3001609 SCOP2B (2022-06-29)
A [auth B]SCOP2B SuperfamilyHead-binding domain of phage P22 tailspike protein8043159 3002008 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth B]Head_bindinge2vkyB1 A: beta sandwichesX: Head-binding domain of phage P22 tailspike protein (From Topology)H: Head-binding domain of phage P22 tailspike protein (From Topology)T: Head-binding domain of phage P22 tailspike proteinF: Head_bindingECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A [auth B]2.170.14.10 Mainly Beta Beta Complex Tailspike Protein ChainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth B]PF09251Salmonella phage P22 tail-spike (PhageP22-tail)Salmonella phage P22 tail-spike- Repeat
A [auth B]PF07716Basic region leucine zipper (bZIP_2)Basic region leucine zipper- Coiled-coil
A [auth B]PF09008Head binding (Head_binding)Head bindingThe head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively an ...The head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively antiparallel. The tailspike protein trimerises through this domain, and the direction of the strands with respect to the molecular triad is almost parallel for beta-sheet A, whereas beta-sheet B is perpendicular to the triad, forming a dome-like structure. This domain is dispensable for thermostability and SDS resistance of the intact protein, and its deletion has only minor effects on tailspike folding kinetics [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth B]TAIL PROTEIN, PIIGCN4