1GG3

CRYSTAL STRUCTURE OF THE PROTEIN 4.1R MEMBRANE BINDING DOMAIN

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)
B	d1gg3b1	All alpha proteins	Acyl-CoA binding protein-like	Second domain of FERM	Second domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1gg3b2	All beta proteins	PH domain-like barrel	PH domain-like	Third domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1gg3b3	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	Ubiquitin-like	First domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gg3c1	All alpha proteins	Acyl-CoA binding protein-like	Second domain of FERM	Second domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gg3c2	All beta proteins	PH domain-like barrel	PH domain-like	Third domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gg3c3	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	Ubiquitin-like	First domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1gg3a1	All alpha proteins	Acyl-CoA binding protein-like	Second domain of FERM	Second domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1gg3a2	All beta proteins	PH domain-like barrel	PH domain-like	Third domain of FERM	Erythroid membrane protein 4.1R	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1gg3a3	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	Ubiquitin-like	First domain of FERM	Erythroid membrane protein 4.1R	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)
B	SCOP2B Superfamily	FERM central domain-like	8036738	3001227	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ubiquitin-like	8034472	3000157	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PH domain-like	8042512	3000134	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	FERM central domain-like	8036738	3001227	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PH domain-like	8042512	3000134	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ubiquitin-like	8034472	3000157	SCOP2B (2022-06-29)
A	SCOP2 Family	FERM domain-like	8024359	4000747	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FERM central domain-like	8036738	3001227	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PH domain-like	8042512	3000134	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Ubiquitin-like	8034472	3000157	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)
B	FERM_C	e1gg3B1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: FERM_C	ECOD (1.6)
B	FERM_M	e1gg3B2	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: FERM_M	ECOD (1.6)
B	FERM_N	e1gg3B3	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: FERM_N	ECOD (1.6)
C	FERM_C	e1gg3C1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: FERM_C	ECOD (1.6)
C	FERM_M	e1gg3C2	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: FERM_M	ECOD (1.6)
C	FERM_N	e1gg3C3	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: FERM_N	ECOD (1.6)
A	FERM_C	e1gg3A1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: FERM_C	ECOD (1.6)
A	FERM_M	e1gg3A2	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: FERM_M	ECOD (1.6)
A	FERM_N	e1gg3A3	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: FERM_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
B	3.10.20.90	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Phosphatidylinositol 3-kinase Catalytic Subunit	CATH (4.3.0)
B	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
C	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
C	3.10.20.90	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Phosphatidylinositol 3-kinase Catalytic Subunit	CATH (4.3.0)
C	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
A	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
A	3.10.20.90	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Phosphatidylinositol 3-kinase Catalytic Subunit	CATH (4.3.0)
A	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF09379	FERM N-terminal domain (FERM_N)	FERM N-terminal domain	This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.	Domain
A, B, C	PF09380	FERM C-terminal PH-like domain (FERM_C)	FERM C-terminal PH-like domain	-	Domain
A, B, C	PF00373	FERM central domain (FERM_M)	FERM central domain	This domain is the central structural domain of the FERM domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	ERYTHROID MEMBRANE PROTEIN 4.1R	cytoskeletal protein binding spectrin binding protein-containing complex binding protein binding binding phosphoprotein binding 1-phosphatidylinositol binding phospholipid binding lipid binding phosphatidylinositol binding actin binding calmodulin binding structural constituent of cytoskeleton structural molecule activity	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis regulation of calcium ion transport regulation of localization regulation of biological process transport regulation of transport regulation of monoatomic ion transport biological regulation cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis regulation of calcium ion transport regulation of localization regulation of biological process transport regulation of transport regulation of monoatomic ion transport biological regulation establishment of localization metal ion transport calcium ion transport localization monoatomic ion transport regulation of metal ion transport monoatomic cation transport cell division organelle organization actomyosin structure organization actin cytoskeleton organization actin filament-based process cytoskeleton organization protein localization positive regulation of protein localization to cell periphery protein localization to cell periphery cellular localization regulation of cellular process regulation of protein localization positive regulation of biological process positive regulation of protein localization to cell cortex regulation of protein localization to cell periphery regulation of cellular localization regulation of protein localization to cell cortex cellular macromolecule localization macromolecule localization positive regulation of protein localization protein localization to cell cortex positive regulation of cellular process cortical actin cytoskeleton organization cortical cytoskeleton organization regulation of protein binding positive regulation of molecular function regulation of molecular function positive regulation of protein binding regulation of binding positive regulation of binding multicellular organismal process system process regulation of intestinal absorption digestive system process regulation of system process regulation of digestive system process digestion intestinal absorption regulation of multicellular organismal process	cellular anatomical structure cell junction cell periphery cell cortex intracellular anatomical structure cytoplasm cytosol plasma membrane membrane basal part of cell basal plasma membrane plasma membrane region basolateral plasma membrane intracellular organelle cellular anatomical structure cell junction cell periphery cell cortex intracellular anatomical structure cytoplasm cytosol plasma membrane membrane basal part of cell basal plasma membrane plasma membrane region basolateral plasma membrane intracellular organelle mitotic spindle cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton protein-containing complex intercellular bridge spectrin-associated cytoskeleton membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear body nucleoplasm organelle lumen nuclear lumen cytoplasmic side of plasma membrane cytoplasmic side of membrane side of membrane cortical cytoskeleton

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR000299	FERM domain	Domain
A, B, C	IPR014352	FERM/acyl-CoA-binding protein superfamily	Homologous Superfamily
A, B, C	IPR019748	FERM central domain	Domain
A, B, C	IPR018980	FERM, C-terminal PH-like domain	Domain
A, B, C	IPR000798	Ezrin/radixin/moesin-like	Family
A, B, C	IPR008379	Band 4.1, C-terminal	Domain
A, B, C	IPR011993	PH-like domain superfamily	Homologous Superfamily
A, B, C	IPR014847	FERM adjacent	Domain
A, B, C	IPR021187	Band 4.1 protein, FERM domain, F1 sub-domain	Domain
A, B, C	IPR019749	Band 4.1 domain	Domain
A, B, C	IPR035963	FERM superfamily, second domain	Homologous Superfamily
A, B, C	IPR019747	FERM conserved site	Conserved Site
A, B, C	IPR018979	FERM, N-terminal	Domain
A, B, C	IPR007477	SAB domain	Domain
A, B, C	IPR029071	Ubiquitin-like domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: P11171	hereditary elliptocytosis elliptocytosis 1 melanoma familial hemolytic anemia congenital anemia pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia cutaneous melanoma large cell medulloblastoma osteosarcoma Cytopenia hemolytic anemia medulloblastoma ovarian cancer

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.