1GN1 | pdb_00001gn1

crystal structure of the mouse CCT gamma apical domain (monoclinic)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d1gn1a_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1gn1b_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d1gn1c_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d1gn1d_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
E	d1gn1e_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
F	d1gn1f_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
G	d1gn1g_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	MOUSE (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
H	d1gn1h_	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	GroEL apical domain-like	Group II chaperonin (CCT, TRIC), apical domain	Thermosome, A-domain	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	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	GroEL apical domain-like	8038745	3000963	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	Cpn60_TCP1_2nd	e1gn1A1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
B	Cpn60_TCP1_2nd	e1gn1B1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
C	Cpn60_TCP1_2nd	e1gn1C1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
D	Cpn60_TCP1_2nd	e1gn1D1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
E	Cpn60_TCP1_2nd	e1gn1E1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
F	Cpn60_TCP1_2nd	e1gn1F1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
G	Cpn60_TCP1_2nd	e1gn1G1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)
H	Cpn60_TCP1_2nd	e1gn1H1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Cpn60_TCP1_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
B	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
C	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
D	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
E	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
F	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
G	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)
H	3.50.7.10	Alpha Beta	3-Layer(bba) Sandwich	GroEL	GroEL	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	CCT-GAMMA	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding unfolded protein binding protein binding 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 ATP-dependent activity ATP-dependent protein folding chaperone protein folding chaperone	regulation of protein stability biological regulation regulation of biological quality protein stabilization positive regulation of organelle organization regulation of cellular process telomere organization regulation of DNA biosynthetic process positive regulation of macromolecule biosynthetic process RNA-templated DNA biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process telomere maintenance via telomere lengthening positive regulation of metabolic process regulation of protein stability biological regulation regulation of biological quality protein stabilization positive regulation of organelle organization regulation of cellular process telomere organization regulation of DNA biosynthetic process positive regulation of macromolecule biosynthetic process RNA-templated DNA biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process telomere maintenance via telomere lengthening positive regulation of metabolic process positive regulation of telomere maintenance via telomere lengthening positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process regulation of biological process positive regulation of telomere maintenance positive regulation of nucleobase-containing compound metabolic process primary metabolic process DNA metabolic process regulation of chromosome organization regulation of telomere maintenance via telomere lengthening regulation of organelle organization positive regulation of chromosome organization telomere maintenance biosynthetic process positive regulation of DNA metabolic process positive regulation of telomere maintenance via telomerase metabolic process regulation of macromolecule biosynthetic process macromolecule metabolic process DNA biosynthetic process regulation of metabolic process regulation of DNA metabolic process regulation of telomere maintenance regulation of cellular component organization positive regulation of cellular component organization positive regulation of biological process cellular component organization nucleic acid biosynthetic process positive regulation of biosynthetic process cellular component organization or biogenesis positive regulation of cellular process regulation of biosynthetic process telomere maintenance via telomerase chromosome organization positive regulation of DNA biosynthetic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process regulation of telomere maintenance via telomerase organelle organization cellular process sperm-egg recognition sexual reproduction cell-cell recognition reproductive process fertilization binding of sperm to zona pellucida cell recognition single fertilization gene expression chaperone-mediated protein folding protein maturation protein folding chaperone mediated protein folding independent of cofactor protein metabolic process 'de novo' protein folding 'de novo' post-translational protein folding	cellular anatomical structure myelin sheath protein-containing complex intracellular anatomical structure protein folding chaperone complex cytoplasm cytosol chaperonin-containing T-complex intracellular protein-containing complex zona pellucida receptor complex cell body polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cellular anatomical structure myelin sheath protein-containing complex intracellular anatomical structure protein folding chaperone complex cytoplasm cytosol chaperonin-containing T-complex intracellular protein-containing complex zona pellucida receptor complex cell body polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027413	GroEL-like equatorial domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR054827	Thermosome subunit alpha	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR017998	Chaperone tailless complex polypeptide 1 (TCP-1)	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027410	TCP-1-like chaperonin intermediate domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR012719	T-complex protein 1, gamma subunit	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR053374	TCP-1 chaperonin-containing T-complex	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002194	Chaperonin TCP-1, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027409	GroEL-like apical domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002423	Chaperonin Cpn60/GroEL/TCP-1 family	Family

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.