Cryo-EM structure of murine Dispatched 'R' conformation. Determined by electron microscopy at 2.5 Å resolution. Released 27 Oct 2021.
Explore 7RPH in 3D Show helices and sheets RCSB PDB PDBe
7RPH contains 56 α-helices and 26 β-strands across 1 chain. 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 | 180-186 | 7 | |
| α-helix | 188-208 | 21 | |
| α-helix | 211-213 | 3 | |
| β-strand | 224 | 1 | 1 |
| α-helix | 228-241 | 14 | |
| β-strand | 243 | 1 | 2 |
| β-strand | 249 | 1 | 2 |
| β-strand | 250 | 1 | 3 |
| α-helix | 254-261 | 8 | |
| β-strand | 299-306 | 8 | 4 |
| α-helix | 315-325 | 11 | |
| α-helix | 326-330 | 5 | |
| α-helix | 335-338 | 4 | |
| β-strand | 341-343 | 3 | 5 |
| β-strand | 346-347 | 2 | 5 |
| α-helix | 348-350 | 3 | |
| β-strand | 351 | 1 | 4 |
| α-helix | 353-360 | 8 | |
| α-helix | 366-368 | 3 | |
| α-helix | 371-389 | 19 | |
| α-helix | 415-418 | 4 | |
| α-helix | 419-421 | 3 | |
| α-helix | 422-425 | 4 | |
| α-helix | 426-430 | 5 | |
| β-strand | 431 | 1 | 4 |
| α-helix | 438-441 | 4 | |
| β-strand | 450-458 | 9 | 4 |
| α-helix | 461-463 | 3 | |
| α-helix | 464-470 | 7 | |
| β-strand | 477 | 1 | 4 |
| β-strand | 481-487 | 7 | 4 |
| α-helix | 492-494 | 3 | |
| α-helix | 495-501 | 7 | |
| α-helix | 504-521 | 18 | |
| α-helix | 524-543 | 20 | |
| α-helix | 544-548 | 5 | |
| α-helix | 556-560 | 5 | |
| α-helix | 561-568 | 8 | |
| α-helix | 571-586 | 16 | |
| α-helix | 592-620 | 29 | |
| α-helix | 621-623 | 3 | |
| β-strand | 626 | 1 | 1 |
| α-helix | 627-647 | 21 | |
| α-helix | 650-657 | 8 | |
| α-helix | 658-662 | 5 | |
| α-helix | 682-702 | 21 | |
| α-helix | 703-707 | 5 | |
| α-helix | 708-714 | 7 | |
| α-helix | 716-735 | 20 | |
| α-helix | 739-743 | 5 | |
| α-helix | 747-749 | 3 | |
| β-strand | 753 | 1 | 6 |
| α-helix | 758-764 | 7 | |
| α-helix | 766-768 | 3 | |
| α-helix | 771-778 | 8 | |
| β-strand | 782-789 | 8 | 3 |
| β-strand | 791 | 1 | 7 |
| β-strand | 810 | 1 | 7 |
| α-helix | 819-833 | 15 | |
| β-strand | 838 | 1 | 8 |
| α-helix | 850-858 | 9 | |
| α-helix | 866-871 | 6 | |
| α-helix | 881-898 | 18 | |
| β-strand | 910-912 | 3 | 3 |
| β-strand | 918-926 | 9 | 3 |
| β-strand | 927 | 1 | 8 |
| β-strand | 928-930 | 3 | 3 |
| α-helix | 931 | 1 | |
| α-helix | 935-953 | 19 | |
| α-helix | 957 | 1 | |
| β-strand | 964-966 | 3 | 3 |
| α-helix | 970-1001 | 32 | |
| β-strand | 1003 | 1 | 9 |
| α-helix | 1004-1027 | 24 | |
| α-helix | 1034-1060 | 27 | |
| α-helix | 1066-1093 | 28 | |
| β-strand | 1100 | 1 | 6 |
| α-helix | 1101-1119 | 19 | |
| α-helix | 1120-1125 | 6 | |
| α-helix | 1126-1132 | 7 | |
| β-strand | 1140 | 1 | 9 |
| α-helix | 1141-1142 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein dispatched homolog 1 | A | protein | 1352 | Mus musculus | Q3TDN0 (AlphaFold model) |
>7RPH_1 Protein dispatched homolog 1 (chains A) MARPFKFPRSYAALLADWPVVVLGMCTLLIVVCALVGVLVPELPDFSDPLLGFEPRGTTI GQRLVTWNNMMRNTGYKATLANYPYKYAEEQARSHRDDRWSDDHHERERREVDWNFQKDS FFCDVPSDGYSRVVFASAGGETLWNLPAIKSMCDVDNSRIRSHPQFSDLCQRTTAVSCCP SWTLGNYIAILNNRSSCQKIVERDVSHTLKLLRTCAKHYQNGTLGPDCWDKAARRKDQLK CTNVPRKCTKYNAVYQILHYLVDKDFMTPKTADYAVPALKYSMLFSPTEKGESMMNIYLD NFENWNSSDGITTVTGIEFGIKHSLFQDYLLMDTVYPAIAIAIVLLIMCVYTKSMFITLM TMFAIISSLIVSYFLYRVVFNFEFFPFMNLTALIILVGIGADDAFVLCDVWNYTKFDKPR AETSEAVSVTLQHAALSMFVTSFTTAAAFYANYVSNITAIRCFGVYAGTAILVNYVLMVT WLPAVIVLHERYLLNIFTCFRKPQPQAYDKSCWAVLCQKCRRVLFAVSEASRIFFEKVLP CIVIKFRYLWLIWFLALTVGGAYIVCVNPKMKLPSLELSEFQVFRSSHPFERYDAEFKKL FMFERVHHGEELHMPITVIWGVSPEDSGDPLNPKSKGELTLDSTFNIASPASQAWILHFC QKLRNQTFFHQTEQQDFTSCFIETFKQWMENQDCDEPALYPCCSHCSFPYKQEVFELCIK KAIMELDRSTGYHLNNKTPGPRFDINDTIRAVVLEFQSTFLFTLAYEKMQQFYKEVDSWI SHELSSAPEGLSRGWFVSNLEFYDLQDSLSDGTLIAMGLSVAVAFSVMLLTTWNIIISLY AIVSIAGTIFVTVGSLVLLGWELNVLESVTISVAVGLSVDFAVHYGVAYRLAPDPDREGK VIFSLSRMGSAIAMAALTTFVAGAMMMPSTVLAYTQLGTFMMLVMCVSWAFATFFFQCLC RCLGPQGTCGQIPFPTKLQCSPFSHTLSARPGDRGPSKTHAASAYSVDARGQKSQLEHEF YELQPLASHSCTSSEKTTYEEPHTCSEFFNGQAKNLRMPVPAAYSSELTKSPSSEPGSAL LQSCLEQDTVCHFSLNPRCNCRDAYTHLQYGLPEIHCQQMGDSLCHKCASTAGGFVQIQS SVAPLKASHQAAEGLLHPAQHMLPPGMQNSRPRNFFLHSVQHFQAQENLGRTSTHSTDER LPRTAELSPPPSDSRSTESFQRACCHPENNQRRLCKSRDPGDTEGSGGTKSKVSGLPNQT DKEEKQVEPSLLQTDETVNSEHLNHNESNFTFSHLPGEAGCRSCPNSPQSCRSIMRSKCG TEDCQTPNLEANVPAVPTHSDLSGESLLIKTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 26 |
| AV0 | Lauryl Maltose Neopentyl Glycol | C47 H88 O22 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
Water and common crystallization additives (NA) are not listed.
Dispatched uses Na + flux to power release of lipid-modified Hedgehog. Wang, Q., Asarnow, D.E., Ding, K. et al. Nature (2021) 599:320-324. DOI 10.1038/s41586-021-03996-0 · PubMed
Other PDB entries of the same protein (UniProt Q3TDN0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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