3GQK

Crystal Structure of the Bacteriophage phi29 gene product 12 C-terminal fragment in complex with ATP

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Bacteriophage phi29 gp12 repeat-like	8105989	3002847	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Bacteriophage phi29 gp12 repeat-like	8105988	3002847	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)
A	PF11962	e3gqkA1	A: beta barrels	X: beta-clip	H: Head decoration protein D (gpD, major capsid protein D) (From Topology)	T: Head decoration protein D (gpD, major capsid protein D)	F: PF11962	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.300.10	Mainly Beta	Beta Barrel	Virus Head Decoration Protein	Chain: A,	CATH (4.3.0)
A	4.10.80.40	Few Secondary Structures	Irregular	Rhinovirus 14, subunit 4	succinate dehydrogenase protein domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF11962	Peptidase_G2, IMC autoproteolytic cleavage domain (Peptidase_G2)	Peptidase_G2, IMC autoproteolytic cleavage domain	This domain is found at the very C-terminus of bacteriophage parallel beta-helical tailspike proteins. It carries the enzymic residues that induce autoproteolytic cleavage to bring about maturation of the folding process of the helix in a chaperone-l ...	This domain is found at the very C-terminus of bacteriophage parallel beta-helical tailspike proteins. It carries the enzymic residues that induce autoproteolytic cleavage to bring about maturation of the folding process of the helix in a chaperone-like manner. The domain thus mediates the assembly of a large tailspike protein and then releases itself after maturation. These C-terminal regions that autoproteolytically release themselves after maturation are exchangeable between functionally unrelated N-terminal proteins and have been identified in a number of bacteriophage tailspike proteins [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Preneck appendage protein	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding	symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms viral life cycle symbiont-mediated disruption of host cell envelope biological process involved in interaction with host biological process involved in symbiotic interaction symbiont entry into host cell via disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell viral process symbiont entry into host disruption of anatomical structure in another organism virion attachment to host cell receptor-mediated virion attachment to host cell symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms viral life cycle symbiont-mediated disruption of host cell envelope biological process involved in interaction with host biological process involved in symbiotic interaction symbiont entry into host cell via disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell viral process symbiont entry into host disruption of anatomical structure in another organism virion attachment to host cell receptor-mediated virion attachment to host cell adhesion of symbiont to host cell adhesion of symbiont to host adhesion receptor-mediated virion attachment to host cell	virus tail, fiber virus tail virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006626	Parallel beta-helix repeat	Repeat
A	IPR012334	Pectin lyase fold	Homologous Superfamily
A	IPR021865	Peptidase G2, IMC autoproteolytic cleavage domain	Domain
A	IPR024535	Pectate lyase superfamily protein	Domain
A	IPR011050	Pectin lyase fold/virulence factor	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.