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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Density map for free recombinant gamma tubulin ring complex | |||||||||
![]() | density map for free recombinant gamma tubulin ring complex | |||||||||
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![]() | Complex / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of transepithelial transport / equatorial microtubule organizing center / morphogenesis of a polarized epithelium / bBAF complex / mitotic spindle microtubule / gamma-tubulin ring complex ...microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of transepithelial transport / equatorial microtubule organizing center / morphogenesis of a polarized epithelium / bBAF complex / mitotic spindle microtubule / gamma-tubulin ring complex / microtubule minus-end binding / interphase microtubule organizing center / postsynaptic actin cytoskeleton organization / protein localization to adherens junction / postsynaptic actin cytoskeleton / polar microtubule / npBAF complex / gamma-tubulin complex / Tat protein binding / brahma complex / structural constituent of postsynaptic actin cytoskeleton / nBAF complex / GBAF complex / meiotic spindle organization / regulation of G0 to G1 transition / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / microtubule nucleation / regulation of nucleotide-excision repair / adherens junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / RHOF GTPase cycle / gamma-tubulin binding / Adherens junctions interactions / non-motile cilium / tight junction / regulation of norepinephrine uptake / Sensory processing of sound by outer hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / apical junction complex / microtubule organizing center / establishment or maintenance of cell polarity / regulation of cyclin-dependent protein serine/threonine kinase activity / maintenance of blood-brain barrier / cortical cytoskeleton / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / pericentriolar material / cell leading edge / Recycling pathway of L1 / regulation of G1/S transition of mitotic cell cycle / cytoplasmic microtubule / kinesin binding / mitotic sister chromatid segregation / brush border / calyx of Held / negative regulation of cell differentiation / positive regulation of double-strand break repair via homologous recombination / mitotic spindle assembly / single fertilization / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / spindle assembly / positive regulation of myoblast differentiation / cytoplasmic microtubule organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / EPHB-mediated forward signaling / substantia nigra development / centriole / AURKA Activation by TPX2 / axonogenesis / mitotic spindle organization / ciliary basal body / meiotic cell cycle / condensed nuclear chromosome / negative regulation of protein binding / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / positive regulation of cell differentiation Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.0 Å | |||||||||
![]() | Aher A / Urnavicius L / Kapoor TM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Rigid body fitted model for free recombinant gamma tubulin ring complex. Authors: Aher A / Urnavicius L / Kapoor TM | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 24.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 26.5 KB 26.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.2 KB | Display | ![]() |
Images | ![]() | 167.3 KB | ||
Masks | ![]() | 190.1 MB | ![]() | |
Filedesc metadata | ![]() | 9.6 KB | ||
Others | ![]() ![]() | 150.5 MB 150.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 907.9 KB | Display | ![]() |
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Full document | ![]() | 907.5 KB | Display | |
Data in XML | ![]() | 20.3 KB | Display | |
Data in CIF | ![]() | 26.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8vrdMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | density map for free recombinant gamma tubulin ring complex | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.32 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: Half map for the free recombinant gamma tubulin ring complex
File | emd_43481_half_map_1.map | ||||||||||||
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Annotation | Half map for the free recombinant gamma tubulin ring complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map for the density map for free...
File | emd_43481_half_map_2.map | ||||||||||||
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Annotation | Half map for the density map for free recombinant gamma tubulin ring complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Gamma tubulin ring complex
Entire | Name: Gamma tubulin ring complex |
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Components |
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-Supramolecule #1: Gamma tubulin ring complex
Supramolecule | Name: Gamma tubulin ring complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #5, #1, #7-#8, #2-#4, #6 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Gamma-tubulin complex component 3
Macromolecule | Name: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 103.710102 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ...String: MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ALSGPAPAPQ SLLPGQSNQA PGVGDCLRQQ LGSRLAWTLT ANQPSSQATT SKGVPSAVSR NMTRSRREGD TG GTMEITE AALVRDILYV FQGIDGKNIK MNNTENCYKV EGKANLSRSL RDTAVRLSEL GWLHNKIRRY TDQRSLDRSF GLV GQSFCA ALHQELREYY RLLSVLHSQL QLEDDQGVNL GLESSLTLRR LLVWTYDPKI RLKTLAALVD HCQGRKGGEL ASAV HAYTK TGDPYMRSLV QHILSLVSHP VLSFLYRWIY DGELEDTYHE FFVASDPTVK TDRLWHDKYT LRKSMIPSFM TMDQS RKVL LIGKSINFLH QVCHDQTPTT KMIAVTKSAE SPQDAADLFT DLENAFQGKI DAAYFETSKY LLDVLNKKYS LLDHMQ AMR RYLLLGQGDF IRHLMDLLKP ELVRPATTLY QHNLTGILET AVRATNAQFD SPEILRRLDV RLLEVSPGDT GWDVFSL DY HVDGPIATVF TRECMSHYLR VFNFLWRAKR MEYILTDIRK GHMCNAKLLR NMPEFSGVLH QCHILASEMV HFIHQMQY Y ITFEVLECSW DELWNKVQQA QDLDHIIAAH EVFLDTIISR CLLDSDSRAL LNQLRAVFDQ IIELQNAQDA IYRAALEEL QRRLQFEEKK KQREIEGQWG VTAAEEEEEN KRIGEFKESI PKMCSQLRIL THFYQGIVQQ FLVLLTTSSD ESLRFLSFRL DFNEHYKAR EPRLRVSLGT RGRRSSHT UniProtKB: Gamma-tubulin complex component 3 |
-Macromolecule #2: TUBGCP6 protein
Macromolecule | Name: TUBGCP6 protein / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 199.732516 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE ...String: MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE CLCHSMIQET LQVMEAAPGT GLPTVGLFSF GDPCGDRFER DTRVSLFGAL VHSRTYDMDV RLGLPPVPDN AD LSGLAIK VPPSVDQWED EGFQSASNLT PDSQSEPSVT PDVDLWEAAL TYEASKRRCW ERVGCPPGHR EEPYLTEAGR DAF DKFCRL HQGELQLLAG GVLQAPQPVL VKECELVKDV LNVLIGVVSA TFSLCQPAQA FVVKRGVHVS GASPESISSL LSEV AEYGT CYTRLSHFSL QPVLDSLYSK GLVFQAFTSG LRRYLQYYRA CVLSTPPTLS LLTIGFLFKK LGRQLRYLAE LCGVG AVLP GTCGGGPRAA FPTGVKLLSY LYQEALHNCS NEHYPVLLSL LKTSCEPYTR FIHDWVYSGV FRDAYGEFMI QVNHEY LSF RDKLYWTHGY VLISKEVEDC VPVFLKHIAH DIYVCGKTIN LLKLCCPRHY LCWSDVPVPR ISVIFSLEEL KEIEKDC AV YVGRMERVAR HSSVSKEEKE LRMEIAKQEL IAHAREAASR VLSALSDRQM SERMALDARK REQFQRLKEQ FVKDQERR Q AARQEELDDD FSYARELRDR ERRLKSLEEE LERKASKLSA EAARREQKAL WRIQRHRLES ARLRFLLEDE KHIQEMLKA VSEAHQPQEP PDVLLSVHPQ VTSPGPEHPE GGQGCDSGSA EQHSPAWDGW NRPGLLTPQP LKPLAVGAGG RGLQQAEGAR PFSDSLSIG DFLPVGPGAE PSVQTGMVPL LEVALQTINL DLPPSAPGEA PAAASTQPSR PQEYDFSTVL RPAVATSPAP G PLQAAECS LGSSGLQLWE DSCGKMDACG SASRETLLPS HPPRRAALEE GSSQPTERLF GQVSGGGLPT GDYASEIAPT RP RWNTHGH VSDASIRVGE NVSDVAPTQP RWNTHGHVSN ASISLGESVS DVAPTRPRWN IHGHVSNASI RVGENVSDVA PTR PRWNTH GHVSNASIRV GENVSDVAPT RPRWNTHGHV SDASISLGES VSDMAPARPR WNTHGHVSDA SISLGESVSD MAPT RPRWN THGHVSDTSI RVGENVSDVA PIRSRCNTHG HVSDASISLG EPVSDVVSTR PRWNTHVPIP PPHMVLGALS PEAEP NTPR PQQSPPGHTS QSALSLGAQS AVLDCGPRLP VEVGPSLSSP SSGCGEGSIS VGENVSDVAP TQPWWPNTPG DSVSEE LGP GRSGDTEDLS PNWPLNSQED TAAQSSPGRG EEAEASAAEA QGGEQAYLAG LAGQYHLERY PDSYESMSEP PIAHLLR PV LPRAFAFPVD PQVQSAADET AVQLSELLTL PVLMKRSITA PLAAHISLVN KAAVDYFFVE LHLEAHYEAL RHFLLMED G EFAQSLSDLL FEKLGAGQTP GELLNPLVLN SVLSKALQCS LHGDTPHASN LSLALKYLPE VFAPNAPDVL SCLELRYKV DWPLNIVITE GCLSKYSGVF SFLLQLKLMM WALKDVCFHL KRTALLSHMA GSVQFRQLQL FKHEMQHFVK VIQGYIANQI LHVTWCEFR ARLATVGDLE EIQRAHAEYL HEAVFRGLLT EKAAPVMNVI HSIFSLVLKF RSQLISQAWG PPGGPRGAEH P NFALMQQS YNTFKYYSHF LFKVVTKLVN RGYQPHLEDF LLRINFNNYY QDA UniProtKB: TUBGCP6 protein |
-Macromolecule #3: Mitotic-spindle organizing protein 1
Macromolecule | Name: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 8.485724 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MASSSGAGAA AAAAAANLNA VRETMDVLLE ISRILNTGLD METLSICVRL CEQGINPEAL SSVIKELRKA TEALKAAENM TS UniProtKB: Mitotic-spindle organizing protein 1 |
-Macromolecule #4: Actin, cytoplasmic 1
Macromolecule | Name: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.78266 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF UniProtKB: Actin, cytoplasmic 1 |
-Macromolecule #5: Isoform 3 of Gamma-tubulin complex component 2
Macromolecule | Name: Isoform 3 of Gamma-tubulin complex component 2 / type: protein_or_peptide / ID: 5 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 105.5815 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK ...String: MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK NSGQHLPIFP AWVYERPALI GDFLIGAGIS TDTALPIVLL GWSLALSPRL KCSGVISAHC GLHLPGTLPL AS QESAVVE DLLYVLVGVD GRYVSAQPLA GRQSRTFLVD PNLDLSIREL VHRILPVAAS YSAVTRFIEE KSSFEYGQVN HAL AAAMRT LVKEHLILVS QLEQLHRQGL LSLQKLWFYI QPAMRTMDIL ASLATSVDKG ECLGGSTLSL LHDRSFSYTG DSQA QELCL YLTKAASAPY FEVLEKWIYR GIIHDPYSEF MVEEHELRKE RIQEDYNDKY WDQRYTIVQQ QIPSFLQKMA DKILS TGKY LNVVRECGHD VTCPVAKEII YTLKERAYVE QIEKAFNYAS KVLLDFLMEE KELVAHLRSI KRYFLMDQGD FFVHFM DLA EEELRKPVED ITPPRLEALL ELALRMSTAN TDPFKDDLKI DLMPHDLITQ LLRVLAIETK QEKAMAHADP TELALSG LE AFSFDYIVKW PLSLIINRKA LTRYQMLFRH MFYCKHVERQ LCSVWISNKT AKQHSLHSAQ WFAGAFTLRQ RMLNFVQN I QYYMMFEVME PTWHILEKNL KSASNIDDVL GHHTGFLDTC LKDCMLTNPE LLKVFSKLMS VCVMFTNCMQ KFTQSMKLD GELGGQTLEH STVLGLPAGA EERARKELAR KHLAEHADTV QLVSGFEATI NKFDKNFSAH LLDLLARLSI YSTSDCEHGM ASVISRLDF NGFYTERLER LSAERSQKAT PQVPVLRGPP APAPRVAVTA Q UniProtKB: Gamma-tubulin complex component 2 |
-Macromolecule #6: Tubulin gamma-1 chain
Macromolecule | Name: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 6 / Number of copies: 14 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 52.022617 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT ...String: MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT YSVFPNQDEM SDVVVQPYNS LLTLKRLTQN ADCVVVLDNT ALNRIATDRL HIQNPSFSQI NQLVSTIMSA ST TTLRYPG YMNNDLIGLI ASLIPTPRLH FLMTGYTPLT TDQSVASVRK TTVLDVMRRL LQPKNVMVST GRDRQTNHCY IAI LNIIQG EVDPTQVHKS LQRIRERKLA NFIPWGPASI QVALSRKSPY LPSAHRVSGL MMANHTSISS LFERTCRQYD KLRK REAFL EQFRKEDMFK DNFDEMDTSR EIVQQLIDEY HAATRPDYIS WGTQEQENLY FQ UniProtKB: Tubulin gamma-1 chain |
-Macromolecule #7: Isoform 2 of Gamma-tubulin complex component 4
Macromolecule | Name: Isoform 2 of Gamma-tubulin complex component 4 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 76.108898 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV ...String: MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV RSALEKILAV CHGVMYKQLS AWMLHGLLLD QHEEFFIKQG PSSGNVSAQP EEDEEDLGIG GLTGKQLREL QD LRLIEEE NMLAPSLKQF SLRVEILPSY IPVRVAEKIL FVGESVQMFE NQNVNLTRKG SILKNQEDTF AAELHRLKQQ PLF SLVDFE QVVDRIRSTV AEHLWKLMVE ESDLLGQLKI IKDFYLLGRG ELFQAFIDTA QHMLKTPPTA VTEHDVNVAF QQSA HKVLL DDDNLLPLLH LTIEYHGKEH KDATQAREGP SRETSPREAP ASGWAALGLS YKVQWPLHIL FTPAVLEKYN VVFKY LLSV RRVQAELQHC WALQMQRKHL KSNQTDAIKW RLRNHMAFLV DNLQYYLQVD VLESQFSQLL HQINSTRDFE SIRLAH DHF LSNLLAQSFI LLKPVFHCLN EILDLCHSFC SLVSQNLGPL DERGAAQLSI LVKGFSRQSS LLFKILSSVR NHQINSD LA QLLLRLDYNK YYTQAGGTLG SFGM UniProtKB: Gamma-tubulin complex component 4 |
-Macromolecule #8: Gamma-tubulin complex component 5
Macromolecule | Name: Gamma-tubulin complex component 5 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 118.367406 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES ...String: MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES EEENDQQPLS REDSGIQVDR TPLEEQDQNG KLDPCISWKD EPDDRSWLEH HVVHQYWTAR PSQFPHSLHL HS NLAAVWD QHLYSSDPLY VPDDRVLVTE TQVIRETLWL LSGVKKLFIF QLIDGKVTVR NNIIVTHLTH SCLRSVLEQI AAY GQVVFR LQEFIDEVMG HSSESMLPGS GSVPKKSTEA PFRTYQAFMW ALYKYFISFK EELAEIEKCI INNDTTITLA IVVD KLAPR LSQLKVLHKV FSTGVAEVPP DTRNVVRASH LLNTLYKAIL EYDNVGEASE QTVSLLFSLW VETVRPYLQT VDEWI VHGH LWDGAREFII QRNKNVPVNH RDFWYATYTL YSVSEKTENE EKMSDNASAS SGSDQGPSSR QHTMVSFLKP VLKQII MAG KSMQLLKNLQ CAESTTCQAG ARDAERKSLY TLFLESVQSR LRHGEDSTPQ VLTEQQATKE NLMKMQSIAE SHLELDD VH DPLLAINFAR MYLEQSDFHE KFAGGDVCVD RSSESVTCQT FELTLRSCLY PHIDKQYLDC CGNLMQTLKK DYRLVEYL Q AMRNFFLMEG GDTMYDFYTS IFDKIREKET WQNVSFLNVQ LQEAVGQRYP EDSSRLSISF ENVDTAKKKL PVHILDGLT LSYKVPWPVD IVISLECQKI YNQVFLLLLQ IKWAKYSLDV LLFGELVSTA EKPRLKEGLI HEQDTVAQFG PQKEPVRQQI HRMFLLRVK LMHFVNSLHN YIMTRILHST GLEFQHQVEE AKDLDQLIKI HYRYLSTIHD RCLLREKVSF VKEAIMKVLN L ALMFADGW QAGLGTWRME SIEKMESDFK NCHMFLVTIL NKAVCRGSFP HLESLALSLM AGMEQS UniProtKB: Gamma-tubulin complex component 5 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 6.8 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-8vrd: |