4YDX

Crystal structure of cisplatin bound to a human copper chaperone (monomer) - new refinement

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4ydxa_	Alpha and beta proteins (a+b)	Ferredoxin-like	HMA, heavy metal-associated domain	HMA, heavy metal-associated domain	ATX1 metallochaperone protein (ATOX1)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	HMA, heavy metal-associated domain	8035503	3001159	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	HMA_1	e4ydxA1	A: a+b two layers	X: Alpha-beta plaits	H: HMA-related	T: HMA, heavy metal-associated domain	F: HMA_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00403	Heavy-metal-associated domain (HMA)	Heavy-metal-associated domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Copper transport protein ATOX1	cation binding cuprous ion binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding metallochaperone activity molecular carrier activity copper chaperone activity protein binding copper-dependent protein binding	inorganic ion homeostasis homeostatic process intracellular copper ion homeostasis copper ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis localization transport copper ion transport inorganic ion homeostasis homeostatic process intracellular copper ion homeostasis copper ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis localization transport copper ion transport transition metal ion transport monoatomic ion transport monoatomic cation transport establishment of localization metal ion transport response to oxidative stress response to stimulus response to stress	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017969	Heavy-metal-associated, conserved site	Conserved Site
A	IPR006121	Heavy metal-associated domain, HMA	Domain
A	IPR036163	Heavy metal-associated domain superfamily	Homologous Superfamily
A	IPR051881	Copper transport ATOX1-like	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: O00244	hypertensive disorder acute myeloid leukemia Cryptogenic Chronic Hepatitis ovarian cancer hepatitis lung benign neoplasm Menkes disease Wilson disease osteosarcoma

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.