2A7B

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2a7ba_	All beta proteins	Immunoglobulin-like beta-sandwich	Clathrin adaptor appendage domain	gamma-adaptin C-terminal appendage domain-like	automated matches	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Clathrin adaptor appendage domain	8055293	3002052	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	Alpha_adaptinC2	e2a7bA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Alpha_adaptinC2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1230	Mainly Beta	Sandwich	Immunoglobulin-like	Gamma-adaptin ear (GAE) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02883	Adaptin C-terminal domain (Alpha_adaptinC2)	Adaptin C-terminal domain	Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and ...	Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	gamma-adaptin appendage domain	-	protein localization cellular localization establishment of protein localization nitrogen compound transport transport intracellular transport establishment of localization localization protein transport establishment of localization in cell cellular macromolecule localization macromolecule localization cellular process intracellular protein transport protein localization cellular localization establishment of protein localization nitrogen compound transport transport intracellular transport establishment of localization localization protein transport establishment of localization in cell cellular macromolecule localization macromolecule localization cellular process intracellular protein transport organelle assembly cellular pigmentation pigment granule organization vesicle organization cellular component organization cellular component biogenesis melanosome organization organelle organization pigmentation cellular component assembly cellular component organization or biogenesis melanosome assembly secretion basolateral protein secretion establishment of protein localization to extracellular region export from cell protein secretion protein localization to extracellular region secretion by cell vesicle-mediated transport platelet dense granule organization secretory granule organization endomembrane system organization	membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle clathrin-coated pit membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle clathrin-coated pit membrane vacuolar membrane lytic vacuole vacuole lytic vacuole membrane bounding membrane of organelle lysosomal membrane organelle membrane lysosome Golgi apparatus subcompartment Golgi apparatus organelle subcompartment trans-Golgi network clathrin-coated vesicle coated vesicle trans-Golgi network membrane protein-containing complex vesicle coat membrane protein complex transport vesicle membrane clathrin coat of trans-Golgi network vesicle membrane coat trans-Golgi network transport vesicle membrane trans-Golgi network transport vesicle AP-type membrane coat adaptor complex AP-1 adaptor complex vesicle membrane clathrin vesicle coat Golgi-associated vesicle clathrin-coated vesicle membrane transport vesicle coated membrane clathrin coat coated vesicle membrane cytoplasmic vesicle membrane Golgi-associated vesicle membrane clathrin adaptor complex perinuclear region of cytoplasm presynapse synapse cell junction

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016024	Armadillo-type fold	Homologous Superfamily
A	IPR002553	Clathrin/coatomer adaptor, adaptin-like, N-terminal	Domain
A	IPR017107	Adaptor protein complex AP-1, gamma subunit	Family
A	IPR013041	Clathrin adaptor, appendage, Ig-like subdomain superfamily	Homologous Superfamily
A	IPR050840	Adaptor Complexes Large Subunit	Family
A	IPR011989	Armadillo-like helical	Homologous Superfamily
A	IPR008152	Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain	Domain
A	IPR008153	Gamma-adaptin ear (GAE) domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.