Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4C9B

Crystal structure of eIF4AIII-CWC22 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000184	biological_process	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
A	0000398	biological_process	mRNA splicing, via spliceosome
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0003724	molecular_function	RNA helicase activity
A	0003729	molecular_function	mRNA binding
A	0004386	molecular_function	helicase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005681	cellular_component	spliceosomal complex
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006364	biological_process	rRNA processing
A	0006397	biological_process	mRNA processing
A	0006406	biological_process	mRNA export from nucleus
A	0006417	biological_process	regulation of translation
A	0008143	molecular_function	poly(A) binding
A	0008306	biological_process	associative learning
A	0008380	biological_process	RNA splicing
A	0010629	biological_process	negative regulation of gene expression
A	0016020	cellular_component	membrane
A	0016071	biological_process	mRNA metabolic process
A	0016607	cellular_component	nuclear speck
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0017148	biological_process	negative regulation of translation
A	0030425	cellular_component	dendrite
A	0035145	cellular_component	exon-exon junction complex
A	0035368	molecular_function	selenocysteine insertion sequence binding
A	0035613	molecular_function	RNA stem-loop binding
A	0035640	biological_process	exploration behavior
A	0043021	molecular_function	ribonucleoprotein complex binding
A	0043025	cellular_component	neuronal cell body
A	0045727	biological_process	positive regulation of translation
A	0048701	biological_process	embryonic cranial skeleton morphogenesis
A	0051028	biological_process	mRNA transport
A	0071006	cellular_component	U2-type catalytic step 1 spliceosome
A	0071007	cellular_component	U2-type catalytic step 2 spliceosome
A	0071013	cellular_component	catalytic step 2 spliceosome
A	0071020	cellular_component	post-spliceosomal complex
A	0072715	biological_process	cellular response to selenite ion
A	0090394	biological_process	negative regulation of excitatory postsynaptic potential
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099578	biological_process	regulation of translation at postsynapse, modulating synaptic transmission
A	1904570	biological_process	negative regulation of selenocysteine incorporation
A	1990416	biological_process	cellular response to brain-derived neurotrophic factor stimulus
A	1990904	cellular_component	ribonucleoprotein complex
A	2000622	biological_process	regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
B	0003723	molecular_function	RNA binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 1412

Chain	Residue
A	SER84
A	GLY85
A	THR86
A	GLY87
A	LYS88
A	THR89
A	GOL1419
B	PRO124
B	ARG128

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1413

Chain	Residue
A	PHE58
A	GLU59
A	LYS60
A	HOH2168
A	HOH2169

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1414

Chain	Residue
A	ASP310
A	HOH2134
A	HOH2147
A	HOH2149
B	LEU275
B	THR279
B	GLY311

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1415

Chain	Residue
A	TRP292
A	LYS296

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1407

Chain	Residue
A	ALA55
A	GLY57
A	HOH2031
B	ARG199
B	ASP380
B	ASN383

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1416

Chain	Residue
A	LEU341
A	ILE349
A	ILE365
A	GLY366
A	ARG373
A	HOH2157

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1417

Chain	Residue
A	LYS74
A	ARG76
B	LYS250
B	GLU291

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1418

Chain	Residue
A	VAL304
A	ALA327
B	SER176

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1419

Chain	Residue
A	SER84
A	LYS88
A	THR89
A	ASP187
A	GLU188
A	ILE217
A	PO41412
A	HOH2049
A	HOH2050

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1420

Chain	Residue
A	CYS269
A	TYR272
A	ASP273
B	LYS172

Functional Information from PROSITE/UniProt

site_id	PS00039
Number of Residues	9
Details	DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL

Chain	Residue	Details
A	VAL185-LEU193

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	170
Details	Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Motif: {"description":"Q motif"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Motif: {"description":"DEAD box","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16923391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16931718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19033377","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20479275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HYI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XB2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EX7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	183
Details	Domain: {"description":"MIF4G","evidences":[{"source":"PROSITE-ProRule","id":"PRU00698","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)