4AYT

STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10

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
Pharos: Disease Associations
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	ABC transporter ATPase domain-like	8018399	4003976	SCOP2 (2022-06-29)
A	SCOP2 Family	ABC transporter transmembrane region	8018400	4003811	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ABC transporter-like P-loop ATPases	8057829	3002020	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ABC transporter transmembrane region-like	8057830	3001546	SCOP2 (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	ABC_membrane	e4aytA2	A: alpha bundles	X: Type II ABC exporter transmembrane domain fold	H: Type I ABC exporter transmembrane domain fold (From Topology)	T: Type I ABC exporter transmembrane domain fold	F: ABC_membrane	ECOD (1.6)
A	ABC_tran_1	e4aytA3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: ABC_tran_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.1560.10	Mainly Alpha	Up-down Bundle	ABC transporter transmembrane region fold	ABC transporter type 1, transmembrane domain	CATH (4.3.0)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00664	ABC transporter transmembrane region (ABC_membrane)	ABC transporter transmembrane region	-	Family
A	PF00005	ABC transporter (ABC_tran)	ABC transporter	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are comp ...	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10 MITOCHONDRIAL	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 identical protein binding protein binding protein homodimerization activity protein dimerization activity ABC-type transporter activity active transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity transporter activity transmembrane transporter activity ATP-dependent activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	multicellular organismal process regulation of cellular process cellular developmental process regulation of developmental process homeostatic process positive regulation of biological process cell development regulation of cell differentiation regulation of cell development positive regulation of developmental process multicellular organism development positive regulation of cell differentiation cell differentiation anatomical structure development multicellular organismal process regulation of cellular process cellular developmental process regulation of developmental process homeostatic process positive regulation of biological process cell development regulation of cell differentiation regulation of cell development positive regulation of developmental process multicellular organism development positive regulation of cell differentiation cell differentiation anatomical structure development regulation of immune system process regulation of multicellular organismal process myeloid cell homeostasis positive regulation of cellular process erythrocyte homeostasis developmental process regulation of biological process regulation of multicellular organismal development hemopoiesis regulation of myeloid cell differentiation biological regulation erythrocyte differentiation regulation of erythrocyte differentiation positive regulation of erythrocyte differentiation multicellular organismal-level homeostasis myeloid cell differentiation immune system process positive regulation of myeloid cell differentiation regulation of hemopoiesis homeostasis of number of cells cellular process erythrocyte development myeloid cell development pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process heme biosynthetic process pigment biosynthetic process positive regulation of tetrapyrrole biosynthetic process positive regulation of metabolic process tetrapyrrole biosynthetic process positive regulation of biosynthetic process regulation of tetrapyrrole biosynthetic process porphyrin-containing compound metabolic process positive regulation of heme biosynthetic process regulation of biosynthetic process tetrapyrrole metabolic process regulation of heme biosynthetic process positive regulation of tetrapyrrole metabolic process biosynthetic process regulation of tetrapyrrole metabolic process metabolic process regulation of metabolic process cellular response to stimulus mitochondrial unfolded protein response cellular response to topologically incorrect protein cellular response to stress response to stimulus response to stress response to topologically incorrect protein cellular response to unfolded protein response to unfolded protein localization transport establishment of localization mitochondrial transport positive regulation of protein metabolic process positive regulation of macromolecule biosynthetic process positive regulation of hemoglobin biosynthetic process regulation of primary metabolic process positive regulation of macromolecule metabolic process protein metabolic process hemoglobin metabolic process hemoglobin biosynthetic process regulation of protein metabolic process primary metabolic process regulation of macromolecule metabolic process macromolecule biosynthetic process regulation of hemoglobin biosynthetic process regulation of macromolecule biosynthetic process macromolecule metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017871	ABC transporter-like, conserved site	Conserved Site
A	IPR003439	ABC transporter-like, ATP-binding domain	Domain
A	IPR036640	ABC transporter type 1, transmembrane domain superfamily	Homologous Superfamily
A	IPR003593	AAA+ ATPase domain	Domain
A	IPR011527	ABC transporter type 1, transmembrane domain	Domain
A	IPR039421	Type 1 protein exporter	Family
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9NRK6	colorectal cancer adenoma colorectal carcinoma Malignant neoplasm of breast pancreatic ductal adenocarcinoma breast cancer osteosarcoma rheumatoid arthritis developmental coordination disorder ovarian cancer

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Transmembrane	Alpha-helical polytopic	ABC transporters	Lipid exporter family

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	ATP Binding Cassette (ABC) Transporters	ABCB10 Mitochondrial ABC transporter with bound AMPPC

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.