6VCD

Cryo-EM structure of IRP2-FBXL5-SKP1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
A	0003723	molecular_function	RNA binding
A	0003994	molecular_function	aconitate hydratase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006879	biological_process	intracellular iron ion homeostasis
A	0017148	biological_process	negative regulation of translation
A	0030316	biological_process	osteoclast differentiation
A	0030350	molecular_function	iron-responsive element binding
A	0046872	molecular_function	metal ion binding
A	0048255	biological_process	mRNA stabilization
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0000082	biological_process	G1/S transition of mitotic cell cycle
C	0000209	biological_process	protein polyubiquitination
C	0000785	cellular_component	chromatin
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0006338	biological_process	chromatin remodeling
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0006879	biological_process	intracellular iron ion homeostasis
C	0007346	biological_process	regulation of mitotic cell cycle
C	0008013	molecular_function	beta-catenin binding
C	0010564	biological_process	regulation of cell cycle process
C	0010824	biological_process	regulation of centrosome duplication
C	0014033	biological_process	neural crest cell differentiation
C	0016567	biological_process	protein ubiquitination
C	0019005	cellular_component	SCF ubiquitin ligase complex
C	0019904	molecular_function	protein domain specific binding
C	0030510	biological_process	regulation of BMP signaling pathway
C	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
C	0031507	biological_process	heterochromatin formation
C	0031519	cellular_component	PcG protein complex
C	0032006	biological_process	regulation of TOR signaling
C	0042752	biological_process	regulation of circadian rhythm
C	0042981	biological_process	regulation of apoptotic process
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0050727	biological_process	regulation of inflammatory response
C	0051124	biological_process	synaptic assembly at neuromuscular junction
C	0051298	biological_process	centrosome duplication
C	0051457	biological_process	maintenance of protein location in nucleus
C	0051726	biological_process	regulation of cell cycle
C	0060173	biological_process	limb development
C	0060271	biological_process	cilium assembly
C	0070936	biological_process	protein K48-linked ubiquitination
C	0097602	molecular_function	cullin family protein binding
C	0140677	molecular_function	molecular function activator activity
C	0160072	molecular_function	ubiquitin ligase complex scaffold activity
C	1901524	biological_process	regulation of mitophagy
C	1904415	biological_process	regulation of xenophagy
C	1990444	molecular_function	F-box domain binding
C	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
C	1990757	molecular_function	ubiquitin ligase activator activity
C	2000001	biological_process	regulation of DNA damage checkpoint

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue FES B 800

Chain	Residue
B	CYS662
B	ASP663
B	CYS676
B	CYS686
B	CYS687

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Functional Information from PROSITE/UniProt

site_id	PS00450
Number of Residues	17
Details	ACONITASE_1 Aconitase family signature 1. VviAaVISC.TNNcnpsV

Chain	Residue	Details
A	VAL504-VAL520

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site_id	PS01244
Number of Residues	14
Details	ACONITASE_2 Aconitase family signature 2. GfeIvgyGCSTCVG

Chain	Residue	Details
A	GLY570-GLY583

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Repeat: {"description":"LRR 1"}

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site_id	SWS_FT_FI2
Number of Residues	27
Details	Repeat: {"description":"LRR 2"}

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site_id	SWS_FT_FI3
Number of Residues	27
Details	Repeat: {"description":"LRR 6"}

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site_id	SWS_FT_FI4
Number of Residues	25
Details	Repeat: {"description":"LRR 7"}

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32126207","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VCD","evidenceCode":"ECO:0007744"}]}

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Residue

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

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Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

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