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6VCD

Cryo-EM structure of IRP2-FBXL5-SKP1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0003723molecular_functionRNA binding
A0003994molecular_functionaconitate hydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006417biological_processregulation of translation
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006879biological_processintracellular iron ion homeostasis
A0009791biological_processpost-embryonic development
A0010468biological_processregulation of gene expression
A0017148biological_processnegative regulation of translation
A0030316biological_processosteoclast differentiation
A0030350molecular_functioniron-responsive element binding
A0034101biological_processerythrocyte homeostasis
A0046872molecular_functionmetal ion binding
A0048255biological_processmRNA stabilization
A0050892biological_processintestinal absorption
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0060586biological_processmulticellular organismal-level iron ion homeostasis
C0000209biological_processprotein polyubiquitination
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0006338biological_processchromatin remodeling
C0006511biological_processubiquitin-dependent protein catabolic process
C0006513biological_processprotein monoubiquitination
C0006915biological_processapoptotic process
C0008013molecular_functionbeta-catenin binding
C0016567biological_processprotein ubiquitination
C0019005cellular_componentSCF ubiquitin ligase complex
C0019904molecular_functionprotein domain specific binding
C0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C0031467cellular_componentCul7-RING ubiquitin ligase complex
C0031519cellular_componentPcG protein complex
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0051457biological_processmaintenance of protein location in nucleus
C0061564biological_processaxon development
C0070936biological_processprotein K48-linked ubiquitination
C0097602molecular_functioncullin family protein binding
C0140677molecular_functionmolecular function activator activity
C0160072molecular_functionubiquitin ligase complex scaffold activity
C1904037biological_processpositive regulation of epithelial cell apoptotic process
C1990444molecular_functionF-box domain binding
C1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C1990757molecular_functionubiquitin ligase activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FES B 800
ChainResidue
BCYS662
BASP663
BCYS676
BCYS686
BCYS687

Functional Information from PROSITE/UniProt
site_idPS00450
Number of Residues17
DetailsACONITASE_1 Aconitase family signature 1. VviAaVISC.TNNcnpsV
ChainResidueDetails
AVAL504-VAL520

site_idPS01244
Number of Residues14
DetailsACONITASE_2 Aconitase family signature 2. GfeIvgyGCSTCVG
ChainResidueDetails
AGLY570-GLY583

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues27
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues27
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues25
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32126207","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VCD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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