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- EMDB-25652: GATOR1-RAG-RAGULATOR - Inhibitory Complex -

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Basic information

Entry
Database: EMDB / ID: EMD-25652
TitleGATOR1-RAG-RAGULATOR - Inhibitory Complex
Map dataGATOR1-RAG-RAGULATOR - Inhibitory Complex
Sample
  • Complex: GATOR1-RAG-RAGULATOR - Inhibitory Complex
    • Protein or peptide: x 10 types
  • Ligand: x 1 types
Function / homology
Function and homology information


GATOR1 complex / regulation of cholesterol import / positive regulation of protein localization to lysosome / regulation of cell-substrate junction organization / Gtr1-Gtr2 GTPase complex / regulation of cholesterol efflux / positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding / FNIP-folliculin RagC/D GAP / Ragulator complex / aorta morphogenesis ...GATOR1 complex / regulation of cholesterol import / positive regulation of protein localization to lysosome / regulation of cell-substrate junction organization / Gtr1-Gtr2 GTPase complex / regulation of cholesterol efflux / positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding / FNIP-folliculin RagC/D GAP / Ragulator complex / aorta morphogenesis / protein localization to cell junction / regulation of TORC1 signaling / protein localization to lysosome / TORC1 signaling / regulation of TOR signaling / endosome organization / MTOR signalling / Amino acids regulate mTORC1 / fibroblast migration / lysosome localization / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of TOR signaling / kinase activator activity / cardiac muscle tissue development / protein localization to membrane / enzyme-substrate adaptor activity / vacuolar membrane / azurophil granule membrane / ventricular septum development / endosomal transport / negative regulation of kinase activity / Macroautophagy / regulation of cell size / lysosome organization / small GTPase-mediated signal transduction / roof of mouth development / RHOJ GTPase cycle / RHOQ GTPase cycle / mTORC1-mediated signalling / cellular response to nutrient levels / tertiary granule membrane / RHOH GTPase cycle / CDC42 GTPase cycle / ficolin-1-rich granule membrane / RHOG GTPase cycle / positive regulation of TOR signaling / regulation of receptor recycling / RAC2 GTPase cycle / RAC3 GTPase cycle / response to amino acid / specific granule membrane / positive regulation of autophagy / protein-membrane adaptor activity / negative regulation of TORC1 signaling / positive regulation of TORC1 signaling / tumor necrosis factor-mediated signaling pathway / cellular response to amino acid starvation / RAC1 GTPase cycle / cellular response to starvation / GTPase activator activity / viral genome replication / negative regulation of autophagy / guanyl-nucleotide exchange factor activity / RNA splicing / Regulation of PTEN gene transcription / cholesterol homeostasis / regulation of cell growth / positive regulation of interleukin-8 production / cellular response to amino acid stimulus / TP53 Regulates Metabolic Genes / phosphoprotein binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / response to virus / MAP2K and MAPK activation / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / protein localization / small GTPase binding / positive regulation of protein localization to nucleus / GDP binding / late endosome / glucose homeostasis / E3 ubiquitin ligases ubiquitinate target proteins / GTPase binding / late endosome membrane / positive regulation of NF-kappaB transcription factor activity / positive regulation of canonical NF-kappaB signal transduction / positive regulation of MAPK cascade / lysosome / molecular adaptor activity / endosome membrane / intracellular signal transduction / membrane raft / protein heterodimerization activity / lysosomal membrane / focal adhesion / intracellular membrane-bounded organelle / GTPase activity / DNA-templated transcription / apoptotic process / ubiquitin protein ligase binding
Similarity search - Function
: / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein, C-terminal / Nitrogen Permease regulator of amino acid transport activity 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein C-terminal region / LAMTOR1/MEH1 ...: / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein, C-terminal / Nitrogen Permease regulator of amino acid transport activity 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein C-terminal region / LAMTOR1/MEH1 / Late endosomal/lysosomal adaptor and MAPK and MTOR activator / Late endosomal/lysosomal adaptor and MAPK and MTOR activator / Ragulator complex protein LAMTOR4 / Ragulator complex protein LAMTOR3 / Ragulator complex protein LAMTOR5 / RagA/B / Mitogen-activated protein kinase kinase 1 interacting / Ragulator complex protein LAMTOR5 / Mitogen-activated protein kinase kinase 1 interacting / Gtr1/RagA G protein / RagC/D / Gtr1/RagA G protein conserved region / Ragulator complex protein LAMTOR2-like / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) / DEP domain profile. / Domain found in Dishevelled, Egl-10, and Pleckstrin / DEP domain / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Ragulator complex protein LAMTOR5 / GATOR1 complex protein DEPDC5 / Ragulator complex protein LAMTOR4 / GATOR1 complex protein NPRL3 / Ragulator complex protein LAMTOR1 / Ras-related GTP-binding protein A / GATOR1 complex protein NPRL2 / Ras-related GTP-binding protein C / Ragulator complex protein LAMTOR3 / Ragulator complex protein LAMTOR2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsEgri SB / Shen K
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Mol Cell / Year: 2022
Title: Cryo-EM structures of the human GATOR1-Rag-Ragulator complex reveal a spatial-constraint regulated GAP mechanism.
Authors: Shawn B Egri / Christna Ouch / Hui-Ting Chou / Zhiheng Yu / Kangkang Song / Chen Xu / Kuang Shen /
Abstract: mTORC1 controls cellular metabolic processes in response to nutrient availability. Amino acid signals are transmitted to mTORC1 through the Rag GTPases, which are localized on the lysosomal surface ...mTORC1 controls cellular metabolic processes in response to nutrient availability. Amino acid signals are transmitted to mTORC1 through the Rag GTPases, which are localized on the lysosomal surface by the Ragulator complex. The Rag GTPases receive amino acid signals from multiple upstream regulators. One negative regulator, GATOR1, is a GTPase activating protein (GAP) for RagA. GATOR1 binds to the Rag GTPases via two modes: an inhibitory mode and a GAP mode. How these two binding interactions coordinate to process amino acid signals is unknown. Here, we resolved three cryo-EM structural models of the GATOR1-Rag-Ragulator complex, with the Rag-Ragulator subcomplex occupying the inhibitory site, the GAP site, and both binding sites simultaneously. When the Rag GTPases bind to GATOR1 at the GAP site, both Rag subunits contact GATOR1 to coordinate their nucleotide loading states. These results reveal a potential GAP mechanism of GATOR1 during the mTORC1 inactivation process.
History
DepositionDec 7, 2021-
Header (metadata) releaseApr 6, 2022-
Map releaseApr 6, 2022-
UpdateJun 1, 2022-
Current statusJun 1, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_25652.png

Downloads & links

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Map

FileDownload / File: emd_25652.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationGATOR1-RAG-RAGULATOR - Inhibitory Complex
Voxel sizeX=Y=Z: 0.655 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.42567137 - 0.8935239
Average (Standard dev.)0.002156765 (±0.03221147)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 288.19998 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : GATOR1-RAG-RAGULATOR - Inhibitory Complex

EntireName: GATOR1-RAG-RAGULATOR - Inhibitory Complex
Components
  • Complex: GATOR1-RAG-RAGULATOR - Inhibitory Complex
    • Protein or peptide: GATOR complex protein DEPDC5
    • Protein or peptide: GATOR complex protein NPRL2
    • Protein or peptide: GATOR complex protein NPRL3
    • Protein or peptide: Ras-related GTP-binding protein A
    • Protein or peptide: Ras-related GTP-binding protein C
    • Protein or peptide: Ragulator complex protein LAMTOR1
    • Protein or peptide: Ragulator complex protein LAMTOR2
    • Protein or peptide: Ragulator complex protein LAMTOR3
    • Protein or peptide: Ragulator complex protein LAMTOR4
    • Protein or peptide: Ragulator complex protein LAMTOR5
  • Ligand: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER

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Supramolecule #1: GATOR1-RAG-RAGULATOR - Inhibitory Complex

SupramoleculeName: GATOR1-RAG-RAGULATOR - Inhibitory Complex / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: GATOR complex protein DEPDC5

MacromoleculeName: GATOR complex protein DEPDC5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 181.478 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE DLQKETISVD QTVTQVFRLR PYQDVYVNV VDPKDVTLDL VELTFKDQYI GRGDMWRLKK SLVSTCAYIT QKVEFAGIRA QAGELWVKNE KVMCGYISED T RVVFRSTS ...String:
MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE DLQKETISVD QTVTQVFRLR PYQDVYVNV VDPKDVTLDL VELTFKDQYI GRGDMWRLKK SLVSTCAYIT QKVEFAGIRA QAGELWVKNE KVMCGYISED T RVVFRSTS AMVYIFIQMS CEMWDFDIYG DLYFEKAVNG FLADLFTKWK EKNCSHEVTV VLFSRTFYDA KSVDEFPEIN RA SIRQDHK GRFYEDFYKV VVQNERREEW TSLLVTIKKL FIQYPVLVRL EQAEGFPQGD NSTSAQGNYL EAINLSFNVF DKH YINRNF DRTGQMSVVI TPGVGVFEVD RLLMILTKQR MIDNGIGVDL VCMGEQPLHA VPLFKLHNRS APRDSRLGDD YNIP HWINH SFYTSKSQLF CNSFTPRIKL AGKKPASEKA KNGRDTSLGS PKESENALPI QVDYDAYDAQ VFRLPGPSRA QCLTT CRSV RERESHSRKS ASSCDVSSSP SLPSRTLPTE EVRSQASDDS SLGKSANILM IPHPHLHQYE VSSSLGYTST RDVLEN MME PPQRDSSAPG RFHVGSAESM LHVRPGGYTP QRALINPFAP SRMPMKLTSN RRRWMHTFPV GPSGEAIQIH HQTRQNM AE LQGSGQRDPT HSSAELLELA YHEAAGRHSN SRQPGDGMSF LNFSGTEELS VGLLSNSGAG MNPRTQNKDS LEDSVSTS P DPILTLSAPP VVPGFCCTVG VDWKSLTTPA CLPLTTDYFP DRQGLQNDYT EGCYDLLPEA DIDRRDEDGV QMTAQQVFE EFICQRLMQG YQIIVQPKTQ KPNPAVPPPL SSSPLYSRGL VSRNRPEEED QYWLSMGRTF HKVTLKDKMI TVTRYLPKYP YESAQIHYT YSLCPSHSDS EFVSCWVEFS HERLEEYKWN YLDQYICSAG SEDFSLIESL KFWRTRFLLL PACVTATKRI T EGEAHCDI YGDRPRADED EWQLLDGFVR FVEGLNRIRR RHRSDRMMRK GTAMKGLQMT GPISTHSLES TAPPVGKKGT SA LSALLEM EASQKCLGEQ QAAVHGGKSS AQSAESSSVA MTPTYMDSPR KDGAFFMEFV RSPRTASSAF YPQVSVDQTA TPM LDGTSL GICTGQSMDR GNSQTFGNSQ NIGEQGYSST NSSDSSSQQL VASSLTSSST LTEILEAMKH PSTGVQLLSE QKGL SPYCF ISAEVVHWLV NHVEGIQTQA MAIDIMQKML EEQLITHASG EAWRTFIYGF YFYKIVTDKE PDRVAMQQPA TTWHT AGVD DFASFQRKWF EVAFVAEELV HSEIPAFLLP WLPSRPASYA SRHSSFSRSF GGRSQAAALL AATVPEQRTV TLDVDV NNR TDRLEWCSCY YHGNFSLNAA FEIKLHWMAV TAAVLFEMVQ GWHRKATSCG FLLVPVLEGP FALPSYLYGD PLRAQLF IP LNISCLLKEG SEHLFDSFEP ETYWDRMHLF QEAIAHRFGF VQDKYSASAF NFPAENKPQY IHVTGTVFLQ LPYSKRKF S GQQRRRRNST SSTNQNMFCE ERVGYNWAYN TMLTKTWRSS ATGDEKFADR LLKDFTDFCI NRDNRLVTFW TSCLEKMHA SAP

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Macromolecule #2: GATOR complex protein NPRL2

MacromoleculeName: GATOR complex protein NPRL2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 43.711395 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGSGCRIECI FFSEFHPTLG PKITYQVPED FISRELFDTV QVYIITKPEL QNKLITVTAM EKKLIGCPVC IEHKKYSRNA LLFNLGFVC DAQAKTCALE PIVKKLAGYL TTLELESSFV SMEESKQKLV PIMTILLEEL NASGRCTLPI DESNTIHLKV I EQRPDPPV ...String:
MGSGCRIECI FFSEFHPTLG PKITYQVPED FISRELFDTV QVYIITKPEL QNKLITVTAM EKKLIGCPVC IEHKKYSRNA LLFNLGFVC DAQAKTCALE PIVKKLAGYL TTLELESSFV SMEESKQKLV PIMTILLEEL NASGRCTLPI DESNTIHLKV I EQRPDPPV AQEYDVPVFT KDKEDFFNSQ WDLTTQQILP YIDGFRHIQK ISAEADVELN LVRIAIQNLL YYGVVTLVSI LQ YSNVYCP TPKVQDLVDD KSLQEACLSY VTKQGHKRAS LRDVFQLYCS LSPGTTVRDL IGRHPQQLQH VDERKLIQFG LMK NLIRRL QKYPVRVTRE EQSHPARLYT GCHSYDEICC KTGMSYHELD ERLENDPNII ICWK

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Macromolecule #3: GATOR complex protein NPRL3

MacromoleculeName: GATOR complex protein NPRL3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 63.68082 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRDNTSPISV ILVSSGSRGN KLLFRYPFQR SQEHPASQTS KPRSRYAASN TGDHADEQDG DSRFSDVILA TILATKSEMC GQKFELKID NVRFVGHPTL LQHALGQISK TDPSPKREAP TMILFNVVFA LRANADPSVI NCLHNLSRRI ATVLQHEERR C QYLTREAK ...String:
MRDNTSPISV ILVSSGSRGN KLLFRYPFQR SQEHPASQTS KPRSRYAASN TGDHADEQDG DSRFSDVILA TILATKSEMC GQKFELKID NVRFVGHPTL LQHALGQISK TDPSPKREAP TMILFNVVFA LRANADPSVI NCLHNLSRRI ATVLQHEERR C QYLTREAK LILALQDEVS AMADGNEGPQ SPFHHILPKC KLARDLKEAY DSLCTSGVVR LHINSWLEVS FCLPHKIHYA AS SLIPPEA IERSLKAIRP YHALLLLSDE KSLLGELPID CSPALVRVIK TTSAVKNLQQ LAQDADLALL QVFQLAAHLV YWG KAIIIY PLCENNVYML SPNASVCLYS PLAEQFSHQF PSHDLPSVLA KFSLPVSLSE FRNPLAPAVQ ETQLIQMVVW MLQR RLLIQ LHTYVCLMAS PSEEEPRPRE DDVPFTARVG GRSLSTPNAL SFGSPTSSDD MTLTSPSMDN SSAELLPSGD SPLNQ RMTE NLLASLSEHE RAAILSVPAA QNPEDLRMFA RLLHYFRGRH HLEEIMYNEN TRRSQLLMLF DKFRSVLVVT THEDPV IAV FQALLP

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Macromolecule #4: Ras-related GTP-binding protein A

MacromoleculeName: Ras-related GTP-binding protein A / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 36.615168 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MPNTAMKKKV LLMGKSGSGK TSMRSIIFAN YIARDTRRLG ATIDVEHSHV RFLGNLVLNL WDCGGQDTFM ENYFTSQRDN IFRNVEVLI YVFDVESREL EKDMHYYQSC LEAILQNSPD AKIFCLVHKM DLVQEDQRDL IFKEREEDLR RLSRPLECAC F RTSIWDET ...String:
MPNTAMKKKV LLMGKSGSGK TSMRSIIFAN YIARDTRRLG ATIDVEHSHV RFLGNLVLNL WDCGGQDTFM ENYFTSQRDN IFRNVEVLI YVFDVESREL EKDMHYYQSC LEAILQNSPD AKIFCLVHKM DLVQEDQRDL IFKEREEDLR RLSRPLECAC F RTSIWDET LYKAWSSIVY QLIPNVQQLE MNLRNFAQII EADEVLLFER ATFLVISHYQ CKEQRDVHRF EKISNIIKQF KL SCSKLAA SFQSMEVRNS NFAAFIDIFT SNTYVMVVMS DPSIPSAATL INIRNARKHF EKLERVDGPK HSLLMR

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Macromolecule #5: Ras-related GTP-binding protein C

MacromoleculeName: Ras-related GTP-binding protein C / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.298859 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS KPRILLMGLR RSGKNSIQKV VFHKMSPNE TLFLESTNKI YKDDISNSSF VNFQIWDFPG QMDFFDPTFD YEMIFRGTGA LIYVIDAQDD YMEALTRLHI T VSKAYKVN ...String:
MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS KPRILLMGLR RSGKNSIQKV VFHKMSPNE TLFLESTNKI YKDDISNSSF VNFQIWDFPG QMDFFDPTFD YEMIFRGTGA LIYVIDAQDD YMEALTRLHI T VSKAYKVN PDMNFEVFIH KVDGLSDDHK IETQRDIHQR ANDDLADAGL EKLHLSFYLT SIYDHSIFEA FSKVVQKLIP QL PTLENLL NIFISNSGIE KAFLFDVVSK IYIATDSSPV DMQSYELCCD MIDVVIDVSC IYGLKEDGSG SAYDKESMAI IKL NNTTVL YLKEVTKFLA LVCILREESF ERKGLIDYNF HCFRKAIHEV FEVGVTSHRS CGHQTSASSL KALTHNGTPR NAI

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Macromolecule #6: Ragulator complex protein LAMTOR1

MacromoleculeName: Ragulator complex protein LAMTOR1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.762775 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE QALLSSILAK TASNIIDVSA ADSQGMEQHE YMDRARQYS TRLAVLSSSL THWKKLPPLP SLTSQPHQVL ASEPIPFSDL QQVSRIAAYA YSALSQIRVD AKEELVVQFG I P

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Macromolecule #7: Ragulator complex protein LAMTOR2

MacromoleculeName: Ragulator complex protein LAMTOR2 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.51745 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MLRPKALTQV LSQANTGGVQ STLLLNNEGS LLAYSGYGDT DARVTAAIAS NIWAAYDRNG NQAFNEDNLK FILMDCMEGR VAITRVANL LLCMYAKETV GFGMLKAKAQ ALVQYLEEPL TQVAAS

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Macromolecule #8: Ragulator complex protein LAMTOR3

MacromoleculeName: Ragulator complex protein LAMTOR3 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.637678 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG SKLGLSKNKS IICYYNTYQV VQFNRLPLV VSFIASSSAN TGLIVSLEKE LAPLFEELRQ VVEVS

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Macromolecule #9: Ragulator complex protein LAMTOR4

MacromoleculeName: Ragulator complex protein LAMTOR4 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.753236 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MTSALTQGLE RIPDQLGYLV LSEGAVLASS GDLENDEQAA SAISELVSTA CGFRLHRGMN VPFKRLSVVF GEHTLLVTVS GQRVFVVKR QNRGREPIDV

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Macromolecule #10: Ragulator complex protein LAMTOR5

MacromoleculeName: Ragulator complex protein LAMTOR5 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.6229 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ QAAKLTSDPT DIPVVCLESD NGNIMIQKHD GITVAVHKM AS

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Macromolecule #11: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER

MacromoleculeName: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / type: ligand / ID: 11 / Number of copies: 1 / Formula: GNP
Molecular weightTheoretical: 522.196 Da
Chemical component information

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM / 5'-Guanylyl imidodiphosphate

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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

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: -3.5 µm / Nominal defocus min: -1.0 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 58.3 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 251583

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