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- EMDB-55658: Structure of LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-A... -

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Basic information

Entry
Database: EMDB / ID: EMD-55658
TitleStructure of LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
Map data
Sample
  • Complex: LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
    • Protein or peptide: x 9 types
  • Ligand: x 3 types
KeywordsCullin / E3 ligase / Ubiquitin / LIGASE
Function / homology
Function and homology information


sulfur amino acid biosynthetic process / negative regulation of focal adhesion disassembly / developmental cell growth / Degradation of cysteine and homocysteine / taurine biosynthetic process / cysteine dioxygenase / cysteine dioxygenase activity / response to azide / RBR-type E3 ubiquitin transferase / L-cysteine catabolic process ...sulfur amino acid biosynthetic process / negative regulation of focal adhesion disassembly / developmental cell growth / Degradation of cysteine and homocysteine / taurine biosynthetic process / cysteine dioxygenase / cysteine dioxygenase activity / response to azide / RBR-type E3 ubiquitin transferase / L-cysteine catabolic process / ERBB2 signaling pathway / : / negative regulation of focal adhesion assembly / reelin-mediated signaling pathway / cellular response to camptothecin / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / regulation of neuron migration / target-directed miRNA degradation / elongin complex / protein K11-linked ubiquitination / protein neddylation / response to glucagon / ubiquitin conjugating enzyme binding / NEDD8 ligase activity / response to redox state / : / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / SCF ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / hematopoietic stem cell proliferation / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin ligase complex scaffold activity / nickel cation binding / TGF-beta receptor signaling activates SMADs / regulation of proteolysis / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / response to amino acid / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / regulation of postsynapse assembly / cullin family protein binding / anatomical structure morphogenesis / response to cAMP / ubiquitin ligase complex / protein K63-linked ubiquitination / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / site of DNA damage / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / lactation / endoplasmic reticulum unfolded protein response / protein K48-linked ubiquitination / RNA Polymerase II Pre-transcription Events / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / post-translational protein modification / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / intrinsic apoptotic signaling pathway / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / NF-kB is activated and signals survival / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / response to glucocorticoid / Pexophagy / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation
Similarity search - Function
: / : / : / E3 ubiquitin-protein ligase ARIH2, N-terminal UBA domain / Ariadne domain / Ariadne domain / E3 ubiquitin ligase RBR family / IBR domain, a half RING-finger domain / Nedd8-like ubiquitin / IBR domain ...: / : / : / E3 ubiquitin-protein ligase ARIH2, N-terminal UBA domain / Ariadne domain / Ariadne domain / E3 ubiquitin ligase RBR family / IBR domain, a half RING-finger domain / Nedd8-like ubiquitin / IBR domain / Cysteine dioxygenase type I / Cysteine dioxygenase type I / IBR domain / In Between Ring fingers / TRIAD supradomain / TRIAD supradomain profile. / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Cullin, N-terminal / Cullin protein neddylation domain / : / Cullin, conserved site / Cullin alpha solenoid domain / Cullin family signature. / Elongin-C / Elongin B / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin / : / Cullin alpha+beta domain / Leucine Rich Repeat / Cullin homology domain / Cullin homology domain superfamily / Cullin family profile. / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / RmlC-like cupin domain superfamily / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Leucine-rich repeat profile. / SKP1/BTB/POZ domain superfamily / Ring finger / RmlC-like jelly roll fold / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
E3 ubiquitin-protein ligase ARIH2 / Polyubiquitin-C / Elongin-C / Elongin-B / Ubiquitin-like protein NEDD8 / Cysteine dioxygenase type 1 / Cullin-5 / Leucine-rich repeat-containing protein 58 / RING-box protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.95 Å
AuthorsStier L / Andree GA / Schulman BA
Funding supportEuropean Union, Germany, 2 items
OrganizationGrant numberCountry
European Research Council (ERC)101098161European Union
Boehringer Ingelheim Fonds (BIF) Germany
CitationJournal: Nat Commun / Year: 2026
Title: Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1.
Authors: Gisele A Andree / Luca J Stier / Kerstin Schmiederer / Alina S Thielen / Luis Schmid / Samuel A Maiwald / Karthik V Gottemukkala / Jiale Du / Susanne von Gronau / Claudia Strasser / Judith ...Authors: Gisele A Andree / Luca J Stier / Kerstin Schmiederer / Alina S Thielen / Luis Schmid / Samuel A Maiwald / Karthik V Gottemukkala / Jiale Du / Susanne von Gronau / Claudia Strasser / Judith Müller / Lukas T Henneberg / Camille Guyot / Gary Kleiger / Matthias Mann / Peter J Murray / Brenda A Schulman /
Abstract: Cellular responses to amino acid fluctuations often hinge on ubiquitin-mediated control of metabolic enzymes, yet the underlying E3 ligase pathways remain poorly defined. Using quantitative ...Cellular responses to amino acid fluctuations often hinge on ubiquitin-mediated control of metabolic enzymes, yet the underlying E3 ligase pathways remain poorly defined. Using quantitative proteomics and active cullin-RING ligase (CRL) profiling, we identify LRRC58 as a cysteine-responsive substrate receptor whose stability increases sharply under cysteine starvation. Proteomics reveals an inverse relationship between LRRC58 and the metabolic enzyme cysteine dioxygenase 1 (CDO1), suggesting a cysteine-linked regulatory axis. Biochemical reconstitution and cryo-EM structures show that LRRC58 forms an active CUL2- or CUL5-based CRL that selectively positions CDO1 for ubiquitylation at Lys8. Disease mutant versions of CDO1 mapping to the LRRC58 interface and impaired for the endogenous ubiquitylation pathway were degraded through orthogonal targeting by a VHL-based degrader. Together, our proteomics-guided discovery pipeline, cellular stability studies, and structural analyses uncover a metabolically-tuned LRRC58-CDO1 pathway that links cysteine availability to selective proteasomal turnover, reveals principles of metabolite-regulated CRL activity, and showcases mechanisms distinguishing endogenous and targeted protein degradation.
History
DepositionNov 12, 2025-
Header (metadata) releaseMay 20, 2026-
Map releaseMay 20, 2026-
UpdateMay 20, 2026-
Current statusMay 20, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55658.png

Downloads & links

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Map

FileDownload / File: emd_55658.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 432 pix.
= 367.718 Å		0.85 Å/pix.
x 432 pix.
= 367.718 Å		0.85 Å/pix.
x 432 pix.
= 367.718 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.8512 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0711
Minimum - Maximum-0.32540956 - 0.61998034
Average (Standard dev.)0.00021177591 (±0.0075287567)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions432432432
Spacing432432432
CellA=B=C: 367.71838 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub

EntireName: LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
Components
  • Complex: LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
    • Protein or peptide: Cysteine dioxygenase type 1
    • Protein or peptide: RING-box protein 2
    • Protein or peptide: Ubiquitin
    • Protein or peptide: Elongin-C
    • Protein or peptide: NEDD8
    • Protein or peptide: Cullin-5
    • Protein or peptide: E3 ubiquitin-protein ligase ARIH2
    • Protein or peptide: Elongin-B
    • Protein or peptide: Leucine-rich repeat-containing protein 58
  • Ligand: FE (III) ION
  • Ligand: 5-azanylpentan-2-one
  • Ligand: ZINC ION

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Supramolecule #1: LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub

SupramoleculeName: LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cysteine dioxygenase type 1

MacromoleculeName: Cysteine dioxygenase type 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: cysteine dioxygenase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.867576 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MEQTEVLCPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR NLVDQGNGKF NLMILAWGEG HGSSIHDHT NSHSFLKMLQ GNLKETLFAW PDKKSNEMVK KSERVLRENQ AAYINDSVGL HRVENISHTE PAVSLHLYSP P FDTSHAFD ...String:
MEQTEVLCPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR NLVDQGNGKF NLMILAWGEG HGSSIHDHT NSHSFLKMLQ GNLKETLFAW PDKKSNEMVK KSERVLRENQ AAYINDSVGL HRVENISHTE PAVSLHLYSP P FDTSHAFD QRTGHKNKVT MTFHSKFGIR TPNATSGSLE NN

UniProtKB: Cysteine dioxygenase type 1

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Macromolecule #2: RING-box protein 2

MacromoleculeName: RING-box protein 2 / type: protein_or_peptide / ID: 2 / Details: N-terminal residues 1-4 deleted / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.280944 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
EDGEETCALA SHSGSSGSKS GGDKMFSLKK WNAVAMWSWD VECDTCAICR VQVMDACLRC QAENKQEDCV VVWGECNHSF HNCCMSLWV KQNNRCPLCQ QDWVVQRIGK

UniProtKB: RING-box protein 2

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Macromolecule #3: Ubiquitin

MacromoleculeName: Ubiquitin / type: protein_or_peptide / ID: 3 / Details: contains Ubiquitin residues 1-75 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.519778 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRG

UniProtKB: Polyubiquitin-C

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Macromolecule #4: Elongin-C

MacromoleculeName: Elongin-C / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.485135 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTE IPEFPIAPEI ALELLMAANF LDC

UniProtKB: Elongin-C

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Macromolecule #5: NEDD8

MacromoleculeName: NEDD8 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.573978 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK ILGGSVLHLV LALRGG

UniProtKB: Ubiquitin-like protein NEDD8

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Macromolecule #6: Cullin-5

MacromoleculeName: Cullin-5 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 91.085297 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK IHQALKEDIL EFIKQAQARV LSHQDDTAL LKAYIVEWRK FFTQCDILPK PFCQLEITLM GKQGSNKKSN VEDSIVRKLM LDTWNESIFS NIKNRLQDSA M KLVHAERL ...String:
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK IHQALKEDIL EFIKQAQARV LSHQDDTAL LKAYIVEWRK FFTQCDILPK PFCQLEITLM GKQGSNKKSN VEDSIVRKLM LDTWNESIFS NIKNRLQDSA M KLVHAERL GEAFDSQLVI GVRESYVNLC SNPEDKLQIY RDNFEKAYLD STERFYRTQA PSYLQQNGVQ NYMKYADAKL KE EEKRALR YLETRRECNS VEALMECCVN ALVTSFKETI LAECQGMIKR NETEKLHLMF SLMDKVPNGI EPMLKDLEEH IIS AGLADM VAAAETITTD SEKYVEQLLT LFNRFSKLVK EAFQDDPRFL TARDKAYKAV VNDATIFKLE LPLKQKGVGL KTQP ESKCP ELLANYCDML LRKTPLSKKL TSEEIEAKLK EVLLVLKYVQ NKDVFMRYHK AHLTRRLILD ISADSEIEEN MVEWL REVG MPADYVNKLA RMFQDIKVSE DLNQAFKEMH KNNKLALPAD SVNIKILNAG AWSRSSEKVF VSLPTELEDL IPEVEE FYK KNHSGRKLHW HHLMSNGIIT FKNEVGQYDL EVTTFQLAVL FAWNQRPREK ISFENLKLAT ELPDAELRRT LWSLVAF PK LKRQVLLYEP QVNSPKDFTE GTLFSVNQEF SLIKNAKVQK RGKINLIGRL QLTTERMREE ENEGIVQLRI LRTQEAII Q IMKMRKKISN AQLQTELVEI LKNMFLPQKK MIKEQIEWLI EHKYIRRDES DINTFIYMA

UniProtKB: Cullin-5

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Macromolecule #7: E3 ubiquitin-protein ligase ARIH2

MacromoleculeName: E3 ubiquitin-protein ligase ARIH2 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: RBR-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 57.735695 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ FTCLTYKESE GALNEHMTSL ASVLKVSHS VAKLILVNFH WQVSEILDRY KSNSAQLLVE ARVQPNPSKH VPTSHPPHHC AVCMQFVRKE NLLSLACQHQ F CRSCWEQH ...String:
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ FTCLTYKESE GALNEHMTSL ASVLKVSHS VAKLILVNFH WQVSEILDRY KSNSAQLLVE ARVQPNPSKH VPTSHPPHHC AVCMQFVRKE NLLSLACQHQ F CRSCWEQH CSVLVKDGVG VGVSCMAQDC PLRTPEDFVF PLLPNEELRE KYRRYLFRDY VESHYQLQLC PGADCPMVIR VQ EPRARRV QCNRCNEVFC FKCRQMYHAP TDCATIRKWL TKCADDSETA NYISAHTKDC PKCNICIEKN GGCNHMQCSK CKH DFCWMC LGDWKTHGSE YYECSRYKEN PDIVNQSQQA QAREALKKYL FYFERWENHN KSLQAAAQTY QRIHEKIQER VMNN LGTWI DWQYLQNAAK LLAKCRYTLQ YTYPYAYYME SGPRKKLFEY QQAQLEAEIA NLSWKVERAD SYDRGDLENQ MHIAE QRRR TLLKDFHDT

UniProtKB: E3 ubiquitin-protein ligase ARIH2

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Macromolecule #8: Elongin-B

MacromoleculeName: Elongin-B / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.147781 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALC IEPFSSPPEL PDVMKPQDSG SSANEQAVQ

UniProtKB: Elongin-B

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Macromolecule #9: Leucine-rich repeat-containing protein 58

MacromoleculeName: Leucine-rich repeat-containing protein 58 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.626605 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEEAGAAVVT AGEAELNWSR LSVSTETLES ELEARGEERR GAREALLRLL LPHNRLVSLP RALGSGFPHL QLLDVSGNAL TALGPELLA LRGLRTLLAK NNRLGGPSAL PKGLAQSPLC RSLQVLNLSG NCFQEVPASL LELRALQTLS LGGNQLQSIP A EIENLQSL ...String:
MEEAGAAVVT AGEAELNWSR LSVSTETLES ELEARGEERR GAREALLRLL LPHNRLVSLP RALGSGFPHL QLLDVSGNAL TALGPELLA LRGLRTLLAK NNRLGGPSAL PKGLAQSPLC RSLQVLNLSG NCFQEVPASL LELRALQTLS LGGNQLQSIP A EIENLQSL ECLYLGGNFI KEIPPELGNL PSLNYLVLCD NKIQSIPPQL SQLHSLRSLS LHNNLLTYLP REILNLIHLE EL SLRGNPL VVRFVRDLTY DPPTLLELAA RTIKIRNISY TPYDLPGNLL RYLGSASNCP NPKCGGVYFD CCVRQIKFVD FCG KYRLPL MHYLCSPECS SPCSSASHSS TSQSESDSED EASVAARRMQ KVLLG

UniProtKB: Leucine-rich repeat-containing protein 58

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Macromolecule #10: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 10 / Number of copies: 1 / Formula: FE
Molecular weightTheoretical: 55.845 Da

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Macromolecule #11: 5-azanylpentan-2-one

MacromoleculeName: 5-azanylpentan-2-one / type: ligand / ID: 11 / Number of copies: 1 / Formula: SY8
Molecular weightTheoretical: 101.147 Da
Chemical component information

ChemComp-SY8:
5-azanylpentan-2-one

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Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 8 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.24 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.6 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.95 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 847022
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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