CryoEM structure of Go-coupled NTSR1. Determined by electron microscopy at 2.88 Å resolution. Released 29 Mar 2023.
Explore 8FN1 in 3D Show helices and sheets RCSB PDB PDBe
8FN1 contains 34 α-helices and 62 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 | 61-89 | 29 | |
| α-helix | 102-123 | 22 | |
| α-helix | 124-130 | 7 | |
| α-helix | 138-172 | 35 | |
| α-helix | 174-180 | 7 | |
| α-helix | 183-200 | 18 | |
| α-helix | 204-207 | 4 | |
| β-strand | 208-212 | 5 | 1 |
| β-strand | 223-227 | 5 | 1 |
| α-helix | 231-242 | 12 | |
| α-helix | 243-247 | 5 | |
| α-helix | 248-266 | 19 | |
| α-helix | 303-319 | 17 | |
| α-helix | 322-333 | 12 | |
| α-helix | 341-370 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-28 | 25 | |
| β-strand | 30-37 | 8 | 2 |
| α-helix | 43-45 | 3 | |
| β-strand | 51-52 | 2 | 2 |
| β-strand | 67-73 | 7 | 2 |
| β-strand | 76-82 | 7 | 2 |
| α-helix | 90-92 | 3 | |
| α-helix | 94-97 | 4 | |
| β-strand | 102-108 | 7 | 2 |
| α-helix | 118-126 | 9 | |
| α-helix | 129-131 | 3 | |
| β-strand | 135-141 | 7 | 2 |
| α-helix | 143-149 | 7 | |
| α-helix | 168-180 | 13 | |
| β-strand | 190-194 | 5 | 2 |
| α-helix | 202-222 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-24 | 21 | |
| α-helix | 30-33 | 4 | |
| β-strand | 47-51 | 5 | 3 |
| β-strand | 58-63 | 6 | 4 |
| β-strand | 69-74 | 6 | 4 |
| β-strand | 78-83 | 6 | 4 |
| β-strand | 89-94 | 6 | 4 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 111-116 | 6 | 5 |
| β-strand | 120-125 | 6 | 5 |
| α-helix | 129-131 | 3 | |
| β-strand | 134-140 | 7 | 5 |
| β-strand | 146-153 | 8 | 6 |
| β-strand | 156-161 | 6 | 6 |
| β-strand | 166-170 | 5 | 6 |
| β-strand | 175-180 | 6 | 6 |
| β-strand | 187-192 | 6 | 7 |
| β-strand | 198-203 | 6 | 7 |
| β-strand | 207-212 | 6 | 7 |
| β-strand | 217-222 | 6 | 7 |
| β-strand | 229-234 | 6 | 8 |
| β-strand | 240-245 | 6 | 8 |
| β-strand | 250-254 | 5 | 8 |
| β-strand | 259-264 | 6 | 8 |
| β-strand | 273-278 | 6 | 9 |
| β-strand | 284-289 | 6 | 9 |
| β-strand | 294-298 | 5 | 9 |
| β-strand | 304-308 | 5 | 9 |
| β-strand | 315-320 | 6 | 3 |
| β-strand | 327-331 | 5 | 3 |
| β-strand | 336-339 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-23 | 11 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 10-12 | 3 | 11 |
| β-strand | 17-25 | 9 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 11 |
| β-strand | 45-51 | 7 | 11 |
| β-strand | 58-60 | 3 | 11 |
| β-strand | 68-73 | 6 | 10 |
| β-strand | 78-84 | 7 | 10 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 11 |
| β-strand | 110-111 | 2 | 11 |
| β-strand | 113 | 1 | 10 |
| β-strand | 115-119 | 5 | 11 |
| α-helix | 125-127 | 3 | |
| β-strand | 128-130 | 3 | 12 |
| β-strand | 134-136 | 3 | 13 |
| β-strand | 143-149 | 7 | 12 |
| β-strand | 154 | 1 | 14 |
| β-strand | 160 | 1 | 14 |
| β-strand | 162-167 | 6 | 13 |
| β-strand | 174-178 | 5 | 13 |
| β-strand | 182-183 | 2 | 13 |
| α-helix | 184 | 1 | |
| β-strand | 191-196 | 6 | 12 |
| β-strand | 199-204 | 6 | 12 |
| β-strand | 214-219 | 6 | 13 |
| α-helix | 225 | 1 | |
| β-strand | 226-227 | 2 | 13 |
| β-strand | 231-234 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neurotensin/neuromedin N | F | protein | 6 | Rattus norvegicus | P20068 (AlphaFold model) |
| Neurotensin receptor type 1 | A | protein | 408 | Rattus norvegicus | P20789 (AlphaFold model) |
| Guanine nucleotide-binding protein G(o) subunit alpha | B | protein | 228 | Spodoptera frugiperda, Homo sapiens | P09471 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | C | protein | 358 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | D | protein | 71 | Homo sapiens | P59768 |
| scFv16 | E | protein | 267 | Escherichia coli |
>8FN1_1 Neurotensin/neuromedin N (chains F) RRPYIL
>8FN1_2 Neurotensin receptor type 1 (chains A) MHHHHHHHHHHSDLEVLFQGPLGSGATSESDTAGPNSDLDVNTDIYSKVLVTAIYLALFV VGTVGNSVTLFTLARKKSLQSLQSTVHYHLGSLALSDLLILLLAMPVELYNFIWVHHPWA FGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLA SALLAIPMLFTMGLQNRSADGTHPGGLVCTPIVDTATVKVVIQVNTFMSFLFPMLVISIL NTVIANKLTVMVHQAAEQGRVCTVGTHNGLEHSTFNMTIEPGRVQALRHGVLVLRAVVIA FVVCWLPYHVRRLMFCYISDEQWTTFLFDFYHYFYMLTNALFYASSAINPILYNLVSANF RQVFLSTLACLCPGWRHRRKKRPTFSRKPNSMSSNHAFSTSATRETLY
>8FN1_3 Guanine nucleotide-binding protein G(o) subunit alpha (chains B) MGCTLSAEDKAAVERSKMIEKNLKEDGISAAKDVKLLLLGADNSGKSTIVKQMKIIHGGS GGSGGTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVDLSDYNRMHE SLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYTGPNTYEDAAAYIQA QFESKNRSPNKEIYCHMTCATDTNNAQVIFDAVTDIIIANNLRGCGLY
>8FN1_4 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains C) MHHHHHHLEVLFQGPGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGR IQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMT CAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSG DTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTF TGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSG RLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
>8FN1_5 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains D) MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP FREKKFFCAIL
>8FN1_6 scFv16 (chains E) DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG AGTKLELKAAALEVLFQGPHHHHHHHH
Neurotensin Receptor Allosterism Revealed in Complex with a Biased Allosteric Modulator. Krumm, B.E., DiBerto, J.F., Olsen, R.H.J. et al. Biochemistry (2023) 62:1233-1248. DOI 10.1021/acs.biochem.3c00029 · PubMed
Other PDB entries of the same protein (UniProt P20068 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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