Structure of the Position 7 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain. Determined by electron microscopy at 4.3 Å resolution. Released 2 Oct 2024.
Explore 9G40 in 3D Show helices and sheets RCSB PDB PDBe
9G40 contains 76 α-helices and 16 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 250-261 | 12 | |
| β-strand | 266 | 1 | 1 |
| β-strand | 269 | 1 | 1 |
| β-strand | 270-272 | 3 | 2 |
| β-strand | 277-279 | 3 | 2 |
| α-helix | 282-284 | 3 | |
| α-helix | 288-315 | 28 | |
| α-helix | 322-349 | 28 | |
| α-helix | 367-388 | 22 | |
| α-helix | 397-404 | 8 | |
| α-helix | 412-438 | 27 | |
| α-helix | 462-465 | 4 | |
| α-helix | 471-473 | 3 | |
| α-helix | 480-498 | 19 | |
| α-helix | 533-551 | 19 | |
| α-helix | 552-556 | 5 | |
| α-helix | 558-564 | 7 | |
| α-helix | 565-569 | 5 | |
| α-helix | 574-588 | 15 | |
| β-strand | 591 | 1 | 3 |
| α-helix | 592-594 | 3 | |
| α-helix | 597-610 | 14 | |
| α-helix | 618-623 | 6 | |
| β-strand | 624-628 | 5 | 4 |
| β-strand | 636 | 1 | 3 |
| α-helix | 637-640 | 4 | |
| β-strand | 641-645 | 5 | 4 |
| α-helix | 649-654 | 6 | |
| α-helix | 657-693 | 37 | |
| α-helix | 701-725 | 25 | |
| α-helix | 726-733 | 8 | |
| α-helix | 734-743 | 10 | |
| α-helix | 747-764 | 18 | |
| α-helix | 772-818 | 47 | |
| α-helix | 826-868 | 43 | |
| α-helix | 875-882 | 8 | |
| α-helix | 894-896 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 26-33 | 8 | |
| α-helix | 46-56 | 11 | |
| α-helix | 60-73 | 14 | |
| α-helix | 78-88 | 11 | |
| α-helix | 92-115 | 24 | |
| α-helix | 150-169 | 20 | |
| α-helix | 179-181 | 3 | |
| α-helix | 210-224 | 15 | |
| β-strand | 233-236 | 4 | 5 |
| β-strand | 245-248 | 4 | 5 |
| α-helix | 254-263 | 10 | |
| α-helix | 265-279 | 15 | |
| α-helix | 283-285 | 3 | |
| α-helix | 286-315 | 30 | |
| α-helix | 321-348 | 28 | |
| α-helix | 353-365 | 13 | |
| α-helix | 370-392 | 23 | |
| α-helix | 393-397 | 5 | |
| β-strand | 409-411 | 3 | 6 |
| α-helix | 416-421 | 6 | |
| β-strand | 432-434 | 3 | 6 |
| α-helix | 435 | 1 | |
| α-helix | 441-446 | 6 | |
| α-helix | 447-462 | 16 | |
| α-helix | 473-475 | 3 | |
| α-helix | 482-502 | 21 | |
| α-helix | 503-507 | 5 | |
| α-helix | 509-518 | 10 | |
| α-helix | 525-539 | 15 | |
| β-strand | 542 | 1 | 7 |
| α-helix | 543-545 | 3 | |
| α-helix | 548-560 | 13 | |
| β-strand | 573-577 | 5 | 8 |
| α-helix | 582-590 | 9 | |
| α-helix | 605-607 | 3 | |
| β-strand | 611 | 1 | 7 |
| β-strand | 616-620 | 5 | 8 |
| α-helix | 632-661 | 30 | |
| α-helix | 664-666 | 3 | |
| α-helix | 674-676 | 3 | |
| α-helix | 679-697 | 19 | |
| α-helix | 698-702 | 5 | |
| α-helix | 703-714 | 12 | |
| α-helix | 719-736 | 18 | |
| α-helix | 742-771 | 30 | |
| α-helix | 824-850 | 27 | |
| α-helix | 854-862 | 9 | |
| α-helix | 866-868 | 3 | |
| α-helix | 870-877 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-90 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 60-90 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 35-45 | 11 | |
| α-helix | 57-62 | 6 | |
| α-helix | 67-79 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gamma-tubulin complex component 3 | F | protein | 910 | Sus scrofa | F1RN46 (AlphaFold model) |
| Gamma-tubulin complex component | G | protein | 905 | Sus scrofa | A0A480VJI0 (AlphaFold model) |
| Mitotic-spindle organizing protein 2A isoform X4 | X | protein | 155 | Sus scrofa | F1RK97 (AlphaFold model) |
| CDK5 regulatory subunit-associated protein 2 | u, v | protein | 1893 | Homo sapiens | Q96SN8 (AlphaFold model) |
>9G40_1 Gamma-tubulin complex component 3 (chains F) MATPDQKSPNVLLQNLCCRILGKSEADVAQQFQYAVRVIGSNFAPTVERDEFLVAEKIKK ELTRQRREADAALFSELHRKLHSQGVLKNKWSILYLLLSLSEDPRKQPSKVSGYAALFAQ ALPRDAHSTPYYYARPQSLPLNYQERGAPSAQSAGSAGSSGVSSLGTYALNGPTPPPPPP ALLPGQPLPAPGVGDGLRQQLGSRLAWTLTASQPSLPSTTSKAVPSSGSRGAARPRREGD AAAGAVEVTEAALVRDILYVFQGIDGKHVKMSNADNCYTVEGKANLSKSLRDTAVRLAEL GWLHNKIRKYTDQRSLDRSFGLVGQSFCAALHQELREYYRLLSVLHSQLQLEDDQGVNLG LESSLTLRRLLVWTYDPKMRLKTLAALVDHCQGRKGGELASAVHAYTKTGDPYARSLVQH ILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPAVKADRLWHDKYALRKPMIPSFMTM DQCRKVLLIGKSINFLHQVCHDQTPTTKMIAVTKSAESPQDAADLFTDLENAFQGKIDAA YFETSKYLLDVLNKKYSLLDHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNL TGILETAVRATNAQFDSPEILKRLDVRLLEVSPGDTGWDVFSLDYHVDGPIATVFTRECM SHYLRAFNFLWRAKRVEYILTDIRKGHMCNARLLRSMPEFSGVLHHCHILASEMVHFIHQ MQYYVTFEVLECSWDELWNRVQRAQDLDHIIAAHEAFLGTVISRCLLDSDSRALLNQLRA VFDQIIELQNTQDAIYRAALEELQRRLQFEEKKKQREAEGQWGVSAAEEEQEKRRVQEFQ ESIPKMCSQLRILTHFYQGVVQQFLVSLTTSSDESLRFLSFRLDFNEHYRAREPRLRVSL GTRGRRSSHT
>9G40_2 Gamma-tubulin complex component (chains G) MSEFRIHHDVNELLSLLRVHGGDGAEVYIDLLQKNRTPYVTTTVSAHSAKVKIAEFSRTP EDFLKKYDELKSKNTRNLDPLVYLLSKLMEDRETLQYLQQNAKERAELAASAAASSTASF GASATASKISMQELEELRKQLGSVATGPTWQQSLELTRKMLRDKQSKKNSGQRLPVLPAW VYERPALLGDFLPGTGGSADTAVPIGSLPLASQEAAVVEDLLYVLVGVDGRYISAQPLTG RQGRTFLVDPNLDLSIRELVSRILPVAASYSTVTRFIEEKSSFEYGQVNHALAAAMRTLV KEYLVLVTQLEQLQRQGLLSLQKLWFYIQPAMRSLDILASLATSVDKGECIGGATLSLLH DRSFSYTGDSQAQELCLHLTKAASTPYFEILEKWIYRGIIDDPYSEFMVEEHELRKEKIQ EDYNDKYWDQRYTVVQRQIPSFLQKMAGKVLSTGKYLNVVRECGHDVTCPVAKEVVYTLK ERAYVEQIEKAFSYASKVLLDFLMGEKELLAHLRSIKRYFLMDQGDFFVHFMDLTEEELK KPVDDITPTRLEALLELALRMSTANTDPFKDDLKIDLMPHDLITQLLRVLAIETQQEKAM VHADPTELTLSGLEAFSFDYVVTWPLSLIINRKALTRYQMLFRHMFYCKHVERQLCSVWI SNKAAKRFSLHSAKWFAGAFTLRQRMLNFVQNIQSYMMFEVMEPTWHVLEQNLRSASNID DVLGHHASFLDNCLKDCMLTNPELLRVFSKLMSVCVMFTNCLQRFTQSMKLDSELGHPAL EPGAMLGPPTEAERAEERARKELARKCLAEHVDAPQLASSFEATITKFDKNFSAHLLDLL ARLSIYSTSDCEHGMASVISRLDFNGFYTERLERLSAERSQKAAPPVPGPRGPPALVPRV AVTAQ
>9G40_3 Mitotic-spindle organizing protein 2A isoform X4 (chains X) MAAPGAGPGPGAPPGLEAALQKLALRRKKVLSAEETELFELAQAAGGAMDPEVFKILVDL LKLNVAPLAVFQMLKSMCAGQRLASEPQDPVAVPLPTTSVPETRGRNRGSSALGGGPALA ERSGREGSSQRMPRQPSATRLPKGGGPGKSPTRST
>9G40_4 CDK5 regulatory subunit-associated protein 2 (chains u, v) MMDLVLEEDVTVPGTLSGCSGLVPSVPDDLDGINPNAGLGNGLLPNVSEETVSPTRARNM KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQER EQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEK AFAGTETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCL KEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFEERIQALEEDLR EKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT QEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEK DLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIK HLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIF SKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQLEQDVLS YQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDL IQLVKELYTDNQHLKKTIFDLSCMGFQGNGFPDRLASTEQTELLASKEDEDTIKIGEDDE INFLSDQHLQQSNEIMKDLSKGGCKNGYLRHTESKISDCDGAHAPGCLEEGAFINLLAPL FNEKATLLLESRPDLLKVVRELLLGQLFLTEQEVSGEHLDGKTEKTPKQKGELVHFVQTN SFSKPHDELKLSCEAQLVKAGEVPKVGLKDASVQTVATEGDLLRFKHEATREAWEEKPIN TALSAEHRPENLHGVPGWQAALLSLPGITNREAKKSRLPILIKPSRSLGNMYRLPATQEV VTQLQSQILELQGELKEFKTCNKQLHQKLILAEAVMEGRPTPDKTLLNAQPPVGAAYQDS PGEQKGIKTTSSVWRDKEMDSDQQRSYEIDSEICPPDDLASLPSCKENPEDVLSPTSVAT YLSSKSQPSAKVSVMGTDQSESINTSNETEYLKQKIHDLETELEGYQNFIFQLQKHSQCS EAIITVLCGTEGAQDGLSKPKNGSDGEEMTFSSLHQVRYVKHVKILGPLAPEMIDSRVLE NLKQQLEEQEYKLQKEQNLNMQLFSEIHNLQNKFRDLSPPRYDSLVQSQARELSLQRQQI KDGHGICVISRQHMNTMIKAFEELLQASDVDYCVAEGFQEQLNQCAELLEKLEKLFLNGK SVGVEMNTQNELMERIEEDNLTYQHLLPESPEPSASHALSDYETSEKSFFSRDQKQDNET EKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFAS GSELHSSLTSEIHFLRKQNQALNAMLIKGSRDKQKENDKLRESLSRKTVSLEHLQREYAS VKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQNDKLLQSLRVE LKAYEKLDEEHRRLREASGEGWKGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLK EQLARGAEKAQEGALTLAVQAVSIPEVPLQPDKHDGDKYPMESDNSFDLFDSSQAVTPKS VSETPPLSGNDTDSLSCDSGSSATSTPCVSRLVTGHHLWASKNGRHVLGLIEDYEALLKQ ISQGQRLLAEMDIQTQEAPSSTSQELGTKGPHPAPLSKFVSSVSTAKLTLEEAYRRLKLL WRVSLPEDGQCPLHCEQIGEMKAEVTKLHKKLFEQEKKLQNTMKLLQLSKRQEKVIFDQL VVTHKILRKARGNLELRPGGAHPGTCSPSRPGS
Partial closure of the gamma-tubulin ring complex by CDK5RAP2 activates microtubule nucleation. Xu, Y., Munoz-Hernandez, H., Krutyholowa, R. et al. Dev Cell (2024) 59:3161. DOI 10.1016/j.devcel.2024.09.002 · PubMed
Other PDB entries of the same protein (UniProt F1RN46 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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