Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ANC

Mechanism of eIF6 release from the nascent 60S ribosomal subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003735	molecular_function	structural constituent of ribosome
A	0005737	cellular_component	cytoplasm
A	0005840	cellular_component	ribosome
A	0006412	biological_process	translation
A	0022625	cellular_component	cytosolic large ribosomal subunit
A	0031012	cellular_component	extracellular matrix
A	1990904	cellular_component	ribonucleoprotein complex
B	0002181	biological_process	cytoplasmic translation
B	0003735	molecular_function	structural constituent of ribosome
B	0005840	cellular_component	ribosome
B	0006412	biological_process	translation
B	0019843	molecular_function	rRNA binding
B	0022625	cellular_component	cytosolic large ribosomal subunit
B	0031012	cellular_component	extracellular matrix
B	0045335	cellular_component	phagocytic vesicle
B	1990904	cellular_component	ribonucleoprotein complex
D	0003735	molecular_function	structural constituent of ribosome
D	0005840	cellular_component	ribosome
D	0006412	biological_process	translation
D	0022625	cellular_component	cytosolic large ribosomal subunit
D	0070180	molecular_function	large ribosomal subunit rRNA binding
D	1990904	cellular_component	ribonucleoprotein complex
E	0003735	molecular_function	structural constituent of ribosome
E	0005840	cellular_component	ribosome
E	0006412	biological_process	translation
E	0022625	cellular_component	cytosolic large ribosomal subunit
E	0031012	cellular_component	extracellular matrix
E	0070180	molecular_function	large ribosomal subunit rRNA binding
E	1990904	cellular_component	ribonucleoprotein complex
F	0003735	molecular_function	structural constituent of ribosome
F	0005811	cellular_component	lipid droplet
F	0005840	cellular_component	ribosome
F	0006412	biological_process	translation
F	0022625	cellular_component	cytosolic large ribosomal subunit
F	1990904	cellular_component	ribonucleoprotein complex
G	0003735	molecular_function	structural constituent of ribosome
H	0003735	molecular_function	structural constituent of ribosome
H	0005840	cellular_component	ribosome
H	0006412	biological_process	translation
J	0000922	cellular_component	spindle pole
J	0002244	biological_process	hematopoietic progenitor cell differentiation
J	0003723	molecular_function	RNA binding
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005654	cellular_component	nucleoplasm
J	0005730	cellular_component	nucleolus
J	0005737	cellular_component	cytoplasm
J	0005819	cellular_component	spindle
J	0005829	cellular_component	cytosol
J	0006364	biological_process	rRNA processing
J	0007052	biological_process	mitotic spindle organization
J	0008017	molecular_function	microtubule binding
J	0019843	molecular_function	rRNA binding
J	0030282	biological_process	bone mineralization
J	0030595	biological_process	leukocyte chemotaxis
J	0042254	biological_process	ribosome biogenesis
J	0042256	biological_process	cytosolic ribosome assembly
J	0043022	molecular_function	ribosome binding
J	0048539	biological_process	bone marrow development
K	0000166	molecular_function	nucleotide binding
K	0003746	molecular_function	translation elongation factor activity
K	0003924	molecular_function	GTPase activity
K	0005515	molecular_function	protein binding
K	0005525	molecular_function	GTP binding
K	0005829	cellular_component	cytosol
K	0006412	biological_process	translation
K	0006414	biological_process	translational elongation
K	0016787	molecular_function	hydrolase activity
K	0042254	biological_process	ribosome biogenesis
K	0042256	biological_process	cytosolic ribosome assembly
K	0043022	molecular_function	ribosome binding
K	0046039	biological_process	GTP metabolic process
K	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PROSITE/UniProt

site_id	PS01267
Number of Residues	20
Details	UPF0023 Uncharacterized protein family UPF0023 signature. EkdLDEVLqthsVFvnvsKG

Chain	Residue	Details
J	GLU44-GLY63

site_id	PS00700
Number of Residues	22
Details	RIBOSOMAL_L6_2 Ribosomal protein L6 signature 2. LrsaIkyKdvRkFlDGIYVseR

Chain	Residue	Details
B	LEU161-ARG182

site_id	PS01257
Number of Residues	22
Details	RIBOSOMAL_L10E Ribosomal protein L10e signature. ADRlqtGMRgAFGKPmGtvARV

Chain	Residue	Details
F	ALA108-VAL129

site_id	PS01073
Number of Residues	18
Details	RIBOSOMAL_L24E Ribosomal protein L24e signature. YsEfkIyPArGmkFvRgD

Chain	Residue	Details
G	TYR8-ASP25

site_id	PS00474
Number of Residues	24
Details	RIBOSOMAL_L3 Ribosomal protein L3 signature. FaeneliDviGvTkGKGfnGvikR

Chain	Residue	Details
A	PHE212-ARG235

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	122
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	32
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	11
Details	Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	255
Details	Domain: {"description":"tr-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	14
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)