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- EMDB-67234: Overall structure of the human UBR4-KCMF1-Calmodulin complex -

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Basic information

Entry
Database: EMDB / ID: EMD-67234
TitleOverall structure of the human UBR4-KCMF1-Calmodulin complex
Map data
Sample
  • Complex: Human UBR4-KCMF1-Calmodulin complex
    • Protein or peptide: E3 ubiquitin-protein ligase UBR4
    • Protein or peptide: E3 ubiquitin-protein ligase KCMF1
    • Protein or peptide: Calmodulin-1
  • Ligand: CALCIUM ION
KeywordsUbiquitinalytion / LIGASE
Function / homology
Function and homology information


negative regulation of HRI-mediated signaling / synaptic signaling / ubiquitin-dependent protein catabolic process via the N-end rule pathway / HRI-mediated signaling / cytoplasm protein quality control by the ubiquitin-proteasome system / protein branched polyubiquitination / negative regulation of fatty acid biosynthetic process / endosome organization / cytoplasm protein quality control / protein K11-linked ubiquitination ...negative regulation of HRI-mediated signaling / synaptic signaling / ubiquitin-dependent protein catabolic process via the N-end rule pathway / HRI-mediated signaling / cytoplasm protein quality control by the ubiquitin-proteasome system / protein branched polyubiquitination / negative regulation of fatty acid biosynthetic process / endosome organization / cytoplasm protein quality control / protein K11-linked ubiquitination / CaM pathway / Cam-PDE 1 activation / protein K27-linked ubiquitination / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / CaMK IV-mediated phosphorylation of CREB / CASP4 inflammasome assembly / Glycogen breakdown (glycogenolysis) / negative regulation of ryanodine-sensitive calcium-release channel activity / Activation of RAC1 downstream of NMDARs / organelle localization by membrane tethering / CLEC7A (Dectin-1) induces NFAT activation / : / negative regulation of high voltage-gated calcium channel activity / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / Synthesis of IP3 and IP4 in the cytosol / Phase 0 - rapid depolarisation / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / calcineurin-mediated signaling / RHO GTPases activate PAKs / protein quality control for misfolded or incompletely synthesized proteins / regulation of cell communication by electrical coupling involved in cardiac conduction / tertiary granule membrane / Uptake and function of anthrax toxins / Ion transport by P-type ATPases / protein phosphatase activator activity / Long-term potentiation / ficolin-1-rich granule membrane / Calcineurin activates NFAT / regulation of ryanodine-sensitive calcium-release channel activity / DARPP-32 events / Regulation of MECP2 expression and activity / Smooth Muscle Contraction / detection of calcium ion / regulation of cardiac muscle contraction / cellular response to interferon-beta / specific granule membrane / protein K63-linked ubiquitination / Dengue virus activates/modulates innate and adaptive immune responses / presynaptic cytosol / RHO GTPases activate IQGAPs / catalytic complex / calcium channel inhibitor activity / ubiquitin-like ligase-substrate adaptor activity / eNOS activation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Activation of AMPK downstream of NMDARs / Ion homeostasis / regulation of heart rate / Protein methylation / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / titin binding / protein K48-linked ubiquitination / calcium channel complex / voltage-gated potassium channel complex / FCERI mediated Ca+2 mobilization / substantia nigra development / positive regulation of autophagy / FCGR3A-mediated IL10 synthesis / protein serine/threonine kinase activator activity / sperm midpiece / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of receptor signaling pathway via JAK-STAT / calyx of Held / Ras activation upon Ca2+ influx through NMDA receptor / adenylate cyclase activator activity / regulation of cytokinesis / VEGFR2 mediated cell proliferation / spindle microtubule / VEGFR2 mediated vascular permeability / sarcomere / calcium channel regulator activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / myelin sheath / cellular response to type II interferon / Transcriptional activation of mitochondrial biogenesis / long-term synaptic potentiation / Enterobacterial factors antagonize host defense / RAF activation
Similarity search - Function
E3 ubiquitin-protein ligase UBR4, N-terminal / : / E3 ubiquitin-protein ligase UBR4 N-terminal / Drought induced 19 protein type, zinc-binding domain / Drought induced 19 protein (Di19), zinc-binding / : / E3 ubiquitin-protein ligase UBR4-like domain / E3 ubiquitin ligase UBR4, C-terminal / E3 ubiquitin ligase UBR4-like / E3 ubiquitin-protein ligase UBR4 ...E3 ubiquitin-protein ligase UBR4, N-terminal / : / E3 ubiquitin-protein ligase UBR4 N-terminal / Drought induced 19 protein type, zinc-binding domain / Drought induced 19 protein (Di19), zinc-binding / : / E3 ubiquitin-protein ligase UBR4-like domain / E3 ubiquitin ligase UBR4, C-terminal / E3 ubiquitin ligase UBR4-like / E3 ubiquitin-protein ligase UBR4 / UBR4 E3 catalytic module profile. / : / Putative zinc finger in N-recognin (UBR box) / Zinc finger, UBR-type / Zinc finger UBR-type profile. / Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway / Zinc finger ZZ-type signature. / Zinc finger, ZZ type / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / zinc finger / : / Zinc finger C2H2 type domain profile. / Zinc finger C2H2-type / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Armadillo-type fold / WD40-repeat-containing domain superfamily
Similarity search - Domain/homology
Calmodulin-1 / E3 ubiquitin-protein ligase UBR4 / E3 ubiquitin-protein ligase KCMF1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.89 Å
AuthorsHu Z / Yan R
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Protein Cell / Year: 2026
Title: Structural and mechanistic insights into the UBR4-KCMF1-Calmodulin complex.
Authors: Ziwei Hu / Zhiheng Liu / Jiali Xu / Baotong Zhang / Renhong Yan /
History
DepositionNov 22, 2025-
Header (metadata) releaseSep 16, 2026-
Map releaseSep 16, 2026-
UpdateSep 16, 2026-
Current statusSep 16, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_67234.png

Downloads & links

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Map

FileDownload / File: emd_67234.map.gz / Format: CCP4 / Size: 536.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 520 pix.
= 430.04 Å		0.83 Å/pix.
x 520 pix.
= 430.04 Å		0.83 Å/pix.
x 520 pix.
= 430.04 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.827 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-1.0677896 - 1.7766395
Average (Standard dev.)0.00069422566 (±0.031765677)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions520520520
Spacing520520520
CellA=B=C: 430.04 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_67234_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_67234_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Human UBR4-KCMF1-Calmodulin complex

EntireName: Human UBR4-KCMF1-Calmodulin complex
Components
  • Complex: Human UBR4-KCMF1-Calmodulin complex
    • Protein or peptide: E3 ubiquitin-protein ligase UBR4
    • Protein or peptide: E3 ubiquitin-protein ligase KCMF1
    • Protein or peptide: Calmodulin-1
  • Ligand: CALCIUM ION

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Supramolecule #1: Human UBR4-KCMF1-Calmodulin complex

SupramoleculeName: Human UBR4-KCMF1-Calmodulin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: E3 ubiquitin-protein ligase UBR4

MacromoleculeName: E3 ubiquitin-protein ligase UBR4 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 576.602375 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MADYKDDDDK SGPDEVDASG RATSGGEEAA AAAPAPGTPA TGADTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE SEILHHEKQ YEPFYSSFVA LSTHYITTVC SLIPRNQLQS VAAACKVLIE FSLLRLENPD EACAVSQKHL ILLIKGLCTG C SRLDRTEI ...String:
MADYKDDDDK SGPDEVDASG RATSGGEEAA AAAPAPGTPA TGADTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE SEILHHEKQ YEPFYSSFVA LSTHYITTVC SLIPRNQLQS VAAACKVLIE FSLLRLENPD EACAVSQKHL ILLIKGLCTG C SRLDRTEI ITFTAMMKSA KLPQTVKTLS DVEDQKELAS PVSPELRQKE VQMNFLNQLT SVFNPRTVAS QPISTQTLVE GE NDEQSST DQASAIKTKN VFIAQNVASL QELGGSEKLL RVCLNLPYFL RYINRFQDAV LANSFFIMPA TVADATAVRN GFH SLVIDV TMALDTLSLP VLEPLNPSRL QDVTVLSLSC LYAGVSVATC MAILHVGSAQ QVRTGSTSSK EDDYESDAAT IVQK CLEIY DMIGQAISSS RRAGGEHYQN FQLLGAWCLL NSLFLILNLS PTALADKGKE KDPLAALRVR DILSRTKEGV GSPKL GPGK GHQGFGVLSV ILANHAIKLL TSLFQDLQVE ALHKGWETDG PPAALSIMAQ STSIQRIQRL IDSVPLMNLL LTLLST SYR KACVLQRQRK GSMSSDASAS TDSNTYYEDD FSSTEEDSSQ DDDSEPILGQ WFEETISPSK EKAAPPPPPP PPPLESS PR VKSPSKQAPG EKGNILASRK DPELFLGLAS NILNFITSSM LNSRNNFIRN YLSVSLSEHH MATLASIIKE VDKDGLKG S SDEEFAAALY HFNHSLVTSD LQSPNLQNTL LQQLGVAPFS EGPWPLYIHP QSLSVLSRLL LIWQHKASAQ GDPDVPECL KVWDRFLSTM KQNALQGVVP SETEDLNVEH LQMLLLIFHN FTETGRRAIL SLFVQIIQEL SVNMDAQMRF VPLILARLLL IFDYLLHQY SKAPVYLFEQ VQHNLLSPPF GWASGSQDSN SRRATTPLYH GFKEVEENWS KHFSSDAVPH PRFYCVLSPE A SEDDLNRL DSVACDVLFS KLVKYDELYA ALTALLAAGS QLDTVRRKEN KNVTALEACA LQYYFLILWR ILGILPPSKT YI NQLSMNS PEMSECDILH TLRWSSRLRI SSYVNWIKDH LIKQGMKAEH ASSLLELAST TKCSSVKYDV EIVEEYFARQ ISS FCSIDC TTILQLHEIP SLQSIYTLDA AISKVQVSLD EHFSKMAAET DPHKSSEITK NLLPATLQLI DTYASFTRAY LLQN FNEEG TTEKPSKEKL QGFAAVLAIG SSRCKANTLG PTLVQNLPSS VQTVCESWNN INTNEFPNIG SWRNAFANDT IPSES YISA VQAAHLGTLC SQSLPLAASL KHTLLSLVRL TGDLIVWSDE MNPPQVIRTL LPLLLESSTE SVAEISSNSL ERILGP AES DEFLARVYEK LITGCYNILA NHADPNSGLD ESILEECLQY LEKQLESSQA RKAMEEFFSD SGELVQIMMA TANENLS AK FCNRVLKFFT KLFQLTEKSP NPSLLHLCGS LAQLACVEPV RLQAWLTRMT TSPPKDSDQL DVIQENRQLL QLLTTYIV R ENSQVGEGVC AVLLGTLTPM ATEMLANGDG TGFPELMVVM ATLASAGQGA GHLQLHNAAV DWLSRCKKYL SQKNVVEKL NANVMHGKHV MILECTCHIM SYLADVTNAL SQSNGQGPSH LSVDGEERAI EVDSDWVEEL AVEEEDSQAE DSDEDSLCNK LCTFTITQK EFMNQHWYHC HTCKMVDGVG VCTVCAKVCH KDHEISYAKY GSFFCDCGAK EDGSCLALVK RTPSSGMSST M KESAFQSE PRISESLVRH ASTSSPADKA KVTISDGKVA DEEKPKKSSL CRTVEGCREE LQNQANFSFA PLVLDMLNFL MD AIQTNFQ QASAVGSSSR AQQALSELHT VEKAVEMTDQ LMVPTLGSQE GAFENVRMNY SGDQGQTIRQ LISAHVLRRV AMC VLSSPH GRRQHLAVSH EKGKITVLQL SALLKQADSS KRKLTLTRLA SAPVPFTVLS LTGNPCKEDY LAVCGLKDCH VLTF SSSGS VSDHLVLHPQ LATGNFIIKA VWLPGSQTEL AIVTADFVKI YDLCVDALSP TFYFLLPSSK IRDVTFLFNE EGKNI IVIM SSAGYIYTQL MEEASSAQQG PFYVTNVLEI NHEDLKDSNS QVAGGGVSVY YSHVLQMLFF SYCQGKSFAA TISRTT LEV LQLFPINIKS SNGGSKTSPA LCQWSEVMNH PGLVCCVQQT TGVPLVVMVK PDTFLIQEIK TLPAKAKIQD MVAIRHT AC NEQQRTTMIL LCEDGSLRIY MANVENTSYW LQPSLQPSSV ISIMKPVRKR KTATITTRTS SQVTFPIDFF EHNQQLTD V EFGGNDLLQV YNAQQIKHRL NSTGMYVANT KPGGFTIEIS NNNSTMVMTG MRIQIGTQAI ERAPSYIEIF GRTMQLNLS RSRWFDFPFT REEALQADKK LNLFIGASVD PAGVTMIDAV KIYGKTKEQF GWPDEPPEEF PSASVSNICP SNLNQSNGTG DSDSAAPTT TSGTVLERLV VSSLEALESC FAVGPIIEKE RNKNAAQELA TLLLSLPAPA SVQQQSKSLL ASLHTSRSAY H SHKDQALL SKAVQCLNTS SKEGKDLDPE VFQRLVITAR SIAIMRPNNL VHFTESKLPQ METEGMDEGK EPQKQLEGDC CS FITQLVN HFWKLHASKP KNAFLAPACL PGLTHIEATV NALVDIIHGY CTCELDCINT ASKIYMQMLL CPDPAVSFSC KQA LIRVLR PRNKRRHVTL PSSPRSNTPM GDKDDDDDDD ADEKMQSSGI PNGGHIRQES QEQSEVDHGD FEMVSESMVL ETAE NVNNG NPSPLEALLA GAEGFPPMLD IPPDADDETM VELAIALSLQ QDQQGSSSSA LGLQSLGLSG QAPSSSSLDA GTLSD TTAS APASDDEGST AATDGSTLRT SPADHGGSVG SESGGSAVDS VAGEHSVSGR SSAYGDATAE GHPAGPGSVS SSTGAI STT TGHQEGDGSE GEGEGETEGD VHTSNRLHMV RLMLLERLLQ TLPQLRNVGG VRAIPYMQVI LMLTTDLDGE DEKDKGA LD NLLSQLIAEL GMDKKDVSKK NERSALNEVH LVVMRLLSVF MSRTKSGSKS SICESSSLIS SATAAALLSS GAVDYCLH V LKSLLEYWKS QQNDEEPVAT SQLLKPHTTS SPPDMSPFFL RQYVKGHAAD VFEAYTQLLT EMVLRLPYQI KKITDTNSR IPPPVFDHSW FYFLSEYLMI QQTPFVRRQV RKLLLFICGS KEKYRQLRDL HTLDSHVRGI KKLLEEQGIF LRASVVTASS GSALQYDTL ISLMEHLKAC AEIAAQRTIN WQKFCIKDDS VLYFLLQVSF LVDEGVSPVL LQLLSCALCG SKVLAALAAS S GSSSASSS SAPVAASSGQ ATTQSKSSTK KSKKEEKEKE KDGETSGSQE DQLCTALVNQ LNKFADKETL IQFLRCFLLE SN SSSVRWQ AHCLTLHIYR NSSKSQQELL LDLMWSIWPE LPAYGRKAAQ FVDLLGYFSL KTPQTEKKLK EYSQKAVEIL RTQ NHILTN HPNSNIYNTL SGLVEFDGYY LESDPCLVCN NPEVPFCYIK LSSIKVDTRY TTTQQVVKLI GSHTISKVTV KIGD LKRTK MVRTINLYYN NRTVQAIVEL KNKPARWHKA KKVQLTPGQT EVKIDLPLPI VASNLMIEFA DFYENYQAST ETLQC PRCS ASVPANPGVC GNCGENVYQC HKCRSINYDE KDPFLCNACG FCKYARFDFM LYAKPCCAVD PIENEEDRKK AVSNIN TLL DKADRVYHQL MGHRPQLENL LCKVNEAAPE KPQDDSGTAG GISSTSASVN RYILQLAQEY CGDCKNSFDE LSKIIQK VF ASRKELLEYD LQQREAATKS SRTSVQPTFT ASQYRALSVL GCGHTSSTKC YGCASAVTEH CITLLRALAT NPALRHIL V SQGLIRELFD YNLRRGAAAM REEVRQLMCL LTRDNPEATQ QMNDLIIGKV STALKGHWAN PDLASSLQYE MLLLTDSIS KEDSCWELRL RCALSLFLMA VNIKTPVVVE NITLMCLRIL QKLIKPPAPT SKKNKDVPVE ALTTVKPYCN EIHAQAQLWL KRDPKASYD AWKKCLPIRG IDGNGKAPSK SELRHLYLTE KYVWRWKQFL SRRGKRTSPL DLKLGHNNWL RQVLFTPATQ A ARQAACTI VEALATIPSR KQQVLDLLTS YLDELSIAGE CAAEYLALYQ KLITSAHWKV YLAARGVLPY VGNLITKEIA RL LALEEAT LSTDLQQGYA LKSLTGLLSS FVEVESIKRH FKSRLVGTVL NGYLCLRKLV VQRTKLIDET QDMLLEMLED MTT GTESET KAFMAVCIET AKRYNLDDYR TPVFIFERLC SIIYPEENEV TEFFVTLEKD PQQEDFLQGR MPGNPYSSNE PGIG PLMRD IKNKICQDCD LVALLEDDSG MELLVNNKII SLDLPVAEVY KKVWCTTNEG EPMRIVYRMR GLLGDATEEF IESLD STTD EEEDEEEVYK MAGVMAQCGG LECMLNRLAG IRDFKQGRHL LTVLLKLFSY CVKVKVNRQQ LVKLEMNTLN VMLGTL NLA LVAEQESKDS GGAAVAEQVL SIMEIILDES NAEPLSEDKG NLLLTGDKDQ LVMLLDQINS TFVRSNPSVL QGLLRII PY LSFGEVEKMQ ILVERFKPYC NFDKYDEDHS GDDKVFLDCF CKIAAGIKNN SNGHQLKDLI LQKGITQNAL DYMKKHIP S AKNLDADIWK KFLSRPALPF ILRLLRGLAI QHPGTQVLIG TDSIPNLHKL EQVSSDEGIG TLAENLLEAL REHPDVNKK IDAARRETRA EKKRMAMAMR QKALGTLGMT TNEKGQVVTK TALLKQMEEL IEEPGLTCCI CREGYKFQPT KVLGIYTFTK RVALEEMEN KPRKQQGYST VSHFNIVHYD CHLAAVRLAR GREEWESAAL QNANTKCNGL LPVWGPHVPE SAFATCLARH N TYLQECTG QREPTYQLNI HDIKLLFLRF AMEQSFSADT GGGGRESNIH LIPYIIHTVL YVLNTTRATS REEKNLQGFL EQ PKEKWVE SAFEVDGPYY FTVLALHILP PEQWRATRVE ILRRLLVTSQ ARAVAPGGAT RLTDKAVKDY SAYRSSLLFW ALV DLIYNM FKKVPTSNTE GGWSCSLAEY IRHNDMPIYE AADKALKTFQ EEFMPVETFS EFLDVAGLLS EITDPESFLK DLLN SVP

UniProtKB: E3 ubiquitin-protein ligase UBR4

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Macromolecule #2: E3 ubiquitin-protein ligase KCMF1

MacromoleculeName: E3 ubiquitin-protein ligase KCMF1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.992348 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD FDLYYGGEAF SVEQPQSFTC PYCGKMGYT ETSLQEHVTS EHAETSTEVI CPICAALPGG DPNHVTDDFA AHLTLEHRAP RDLDESSGVR HVRRMFHPGR G LGGPRARR ...String:
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD FDLYYGGEAF SVEQPQSFTC PYCGKMGYT ETSLQEHVTS EHAETSTEVI CPICAALPGG DPNHVTDDFA AHLTLEHRAP RDLDESSGVR HVRRMFHPGR G LGGPRARR SNMHFTSSST GGLSSSQSSY SPSNREAMDP IAELLSQLSG VRRSAGGQLN SSGPSASQLQ QLQMQLQLER QH AQAARQQ LETARNATRR TNTSSVTTTI TQSTATTNIA NTESSQQTLQ NSQFLLTRLN DPKMSETERQ SMESERADRS LFV QELLLS TLVREESSSS DEDDRGEMAD FGAMGCVDIM PLDVALENLN LKESNKGNEP PPPPL

UniProtKB: E3 ubiquitin-protein ligase KCMF1

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Macromolecule #3: Calmodulin-1

MacromoleculeName: Calmodulin-1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.852545 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREA FRVFDKDGNG YISAAELRHV MTNLGEKLTD EEVDEMIREA DIDGDGQVNY EEFVQMMTAK

UniProtKB: Calmodulin-1

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Macromolecule #4: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: CA
Molecular weightTheoretical: 40.078 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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 1.5625 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.4000000000000001 µm
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.89 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 244291
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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