Cryo-EM structure of the peptide binding domain of human SRP68/72. Determined by electron microscopy at 3.0 Å resolution. Released 7 Feb 2024.
Explore 8QVW in 3D Show helices and sheets RCSB PDB PDBe
8QVW contains 33 α-helices and 0 β-strands across 2 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 | 554-556 | 3 | |
| α-helix | 565-567 | 3 | |
| α-helix | 579-581 | 3 | |
| α-helix | 585-589 | 5 | |
| α-helix | 593-596 | 4 | |
| α-helix | 600-602 | 3 | |
| α-helix | 604-606 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-24 | 14 | |
| α-helix | 28-40 | 13 | |
| α-helix | 45-57 | 13 | |
| α-helix | 61-75 | 15 | |
| α-helix | 81-90 | 10 | |
| α-helix | 94-102 | 9 | |
| α-helix | 109-121 | 13 | |
| α-helix | 125-138 | 14 | |
| α-helix | 144-161 | 18 | |
| α-helix | 176-189 | 14 | |
| α-helix | 193-210 | 18 | |
| α-helix | 223-238 | 16 | |
| α-helix | 242-255 | 14 | |
| α-helix | 261-274 | 14 | |
| α-helix | 279-289 | 11 | |
| α-helix | 294-297 | 4 | |
| α-helix | 300-316 | 17 | |
| α-helix | 321-332 | 12 | |
| α-helix | 341-350 | 10 | |
| α-helix | 355-367 | 13 | |
| α-helix | 369-371 | 3 | |
| α-helix | 372-382 | 11 | |
| α-helix | 389-397 | 9 | |
| α-helix | 406-418 | 13 | |
| α-helix | 422-439 | 18 | |
| α-helix | 444-459 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle subunit SRP68 | A | protein | 577 | Homo sapiens | Q9UHB9 (AlphaFold model) |
| Signal recognition particle subunit SRP72 | B | protein | 674 | Homo sapiens | O76094 (AlphaFold model) |
>8QVW_1 Signal recognition particle subunit SRP68 (chains A) MKEFGDSLSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTLNFKMGNRHKFTG KKVTEELLTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSRLRKAVKHAEELE RLCESNRVDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIYEKLASAFTEEQA VLYNQRVEEISPNIRYCAYNIGDQSAINELMQMRLRSGGTEGLLAEKLEALITQTRAKQA ATMSEVEWRGRTVPVKIDKVRIFLLGLADNEAAIVQAESEETKERLFESMLSECRDAIQV VREELKPDQKQRDYILEGEPGKVSNLQYLHSYLTYIKLSTAIKRNENMAKGLQRALLQQQ PEDDSKRSPRPQDLIRLYDIILQNLVELLQLPGLEEDKAFQKEIGLKTLVFKAYRCFFIA QSYVLVKKWSEALVLYDRVLKYANEVNSDAGAFKNSLKDLPDVQELITQVRSEKCSLQAA AILDANDAHQTETSSSQVKDNKPLVERFETFCLDPSLVTKQANLVHFPPGFQPIPCKPLF FDLALNHVAFPPLEDKLEQKTKSGLTGYIKGIFGFRS
>8QVW_2 Signal recognition particle subunit SRP72 (chains B) SNAMASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQ NGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQ VLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHE LCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQ LQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFK LSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKA IELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYS HEEDIDSAIEVFTQAIQWYQNHQPKSPAHLSLIREAANFKLKYGRKKEAISDLQQLWKQN PKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKV TGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQ IGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATVSASTSNIIPPRHQKPAGAPATKK KQQQKKKKGGKGGW
Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity. Zhong, Y., Feng, J., Koh, A.F. et al. Nucleic Acids Res (2024) 52:5285-5300. DOI 10.1093/nar/gkae107 · PubMed
Other PDB entries of the same protein (UniProt Q9UHB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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