8H4L: DHA-bound FFAR4
DHA-bound FFAR4 in complex with Gq. Determined by electron microscopy at 3.07 Å resolution. Released 21 Jun 2023.
- Method
- Electron microscopy
- Resolution
- 3.07 Å
- Organisms
- Homo sapiens, Lama glama
- Chains
- 5
- Atoms
- 8,171
- Mol. weight
- 145.88 kDa
- Ligands
- HXA
- Released
- 21 Jun 2023
Explore 8H4L in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8H4L contains 39 α-helices and 47 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.
Chain A: 10 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-37 | 22 | |
| β-strand | 41-46 | 6 | 1 |
| α-helix | 53-60 | 8 | |
| β-strand | 207-214 | 8 | 1 |
| β-strand | 217-224 | 8 | 1 |
| α-helix | 236-238 | 3 | |
| β-strand | 243-249 | 7 | 1 |
| α-helix | 266-277 | 12 | |
| α-helix | 280-282 | 3 | |
| β-strand | 286-292 | 7 | 1 |
| α-helix | 294-303 | 10 | |
| α-helix | 308-310 | 3 | |
| α-helix | 313-316 | 4 | |
| α-helix | 332-350 | 19 | |
| β-strand | 359-363 | 5 | 1 |
| α-helix | 371-390 | 20 | |
Chain B: 3 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-24 | 21 | |
| α-helix | 30-33 | 4 | |
| α-helix | 38-39 | 2 | |
| β-strand | 47-51 | 5 | 2 |
| β-strand | 58-63 | 6 | 3 |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 89-94 | 6 | 3 |
| β-strand | 100-105 | 6 | 4 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 120-125 | 6 | 4 |
| β-strand | 134-140 | 7 | 4 |
| β-strand | 146-151 | 6 | 5 |
| β-strand | 156-161 | 6 | 5 |
| β-strand | 165-170 | 6 | 5 |
| β-strand | 176-181 | 6 | 5 |
| β-strand | 189-192 | 4 | 6 |
| β-strand | 198-202 | 5 | 6 |
| β-strand | 207-212 | 6 | 6 |
| β-strand | 218-223 | 6 | 6 |
| β-strand | 229-234 | 6 | 7 |
| β-strand | 240-245 | 6 | 7 |
| β-strand | 250-254 | 5 | 7 |
| β-strand | 259-264 | 6 | 7 |
| β-strand | 273-278 | 6 | 8 |
| β-strand | 284-289 | 6 | 8 |
| β-strand | 294-298 | 5 | 8 |
| β-strand | 304-308 | 5 | 8 |
| β-strand | 315-320 | 6 | 2 |
| β-strand | 327-331 | 5 | 2 |
| β-strand | 336-339 | 4 | 2 |
Chain G: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-22 | 16 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-58 | 3 | |
Chain N: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 9 |
| β-strand | 10-12 | 3 | 10 |
| β-strand | 17-25 | 9 | 9 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 10 |
| β-strand | 45-51 | 7 | 10 |
| β-strand | 58-60 | 3 | 10 |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 78-84 | 7 | 9 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 10 |
| β-strand | 118 | 1 | 10 |
| β-strand | 122-126 | 5 | 10 |
Chain R: 19 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-25 | 4 | |
| α-helix | 36-67 | 32 | |
| α-helix | 73-88 | 16 | |
| α-helix | 89-91 | 3 | |
| α-helix | 92-101 | 10 | |
| α-helix | 108-144 | 37 | |
| α-helix | 152-169 | 18 | |
| α-helix | 172-175 | 4 | |
| β-strand | 177-183 | 7 | 11 |
| α-helix | 184 | 1 | |
| β-strand | 190-196 | 7 | 11 |
| α-helix | 201-212 | 12 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-240 | 23 | |
| α-helix | 241-245 | 5 | |
| α-helix | 252-255 | 4 | |
| α-helix | 259-269 | 11 | |
| α-helix | 272-276 | 5 | |
| α-helix | 278-292 | 15 | |
| α-helix | 300-310 | 11 | |
| α-helix | 313-320 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| engineered mini Galpha-Q subunit | A | protein | 362 | Homo sapiens | P63092 (AlphaFold model), P63096 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 345 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 71 | Homo sapiens | P59768 (AlphaFold model) |
| Nb35 | N | protein | 161 | Lama glama | |
| Free fatty acid receptor 4 | R | protein | 361 | Homo sapiens | Q5NUL3 |
Sequence of entity 1 (A), FASTA
>8H4L_1 engineered mini Galpha-Q subunit (chains A)
MMGCTLSAEDKAAVERSKMIEKQLQKDKQVYRRTLRLLLLGADNSGKSTIVKQMRIYHVN
GYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFM
TAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRV
KTSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQEALND
FKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDP
RVTRAKYFIRKEFVDISTASGDGRHICYPHFTCSVDTENARRIFNDCKDIILQMNLREYN
LV
Sequence of entity 2 (B), FASTA
>8H4L_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MGSLLQSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHL
AKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACG
GLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQ
QTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFF
PNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCN
VWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 3 (G), FASTA
>8H4L_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 4 (N), FASTA
>8H4L_4 Nb35 (chains N)
MKYLLPTAAAGLLLLAAQPAMAQVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVR
QAPGKGLEWVSDISQSGASISYTGSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCAR
CPAPFTRDCFDVTSTTYAYRGQGTQVTVSSAAALEHHHHHH
Sequence of entity 5 (R), FASTA
>8H4L_5 Free fatty acid receptor 4 (chains R)
MSPECARAAGDAPLRSLEQANRTRFPFFSDVKGDHRLVLAAVETTVLVLIFAVSLLGNVC
ALVLVARRRRRGATACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYVMTL
SGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLALIWGYSAVAALPLCVFFRVV
PQRLPGADQEISICTLIWPTIPGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKR
LTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWP
SLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSIIS
G
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| HXA | Docosa-4,7,10,13,16,19-hexaenoic acid | C22 H32 O2 | 1 |
Primary citation
Structural basis of omega-3 fatty acid receptor FFAR4 activation and G protein coupling selectivity. Yin, H., Inoue, A., Ma, Z. et al. Cell Res (2023) 33:644-647. DOI 10.1038/s41422-023-00835-x · PubMed
Other PDB entries of the same protein (UniProt P63092 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7BPH 1.57 Å, Crystal structure of GppNHp-bound GNAS in complex with the cyclic peptide inhibitor GN13
- 6AU6 1.7 Å, Crystal structure of GDP-bound human GNAS R201C mutant
- 8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
- 7E5E 1.95 Å, Crystal structure of GDP-bound GNAS in complex with the cyclic peptide inhibitor GD20
- 7MBX 1.95 Å, Human Cholecystokinin 1 receptor (CCK1R) Gs complex
- 8F0J 2.0 Å, Calcitonin Receptor in complex with Gs and Pramlintide analogue peptide San45
- 8F2B 2.0 Å, Amylin 3 Receptor in complex with Gs and Pramlintide analogue peptide San45
- 9XXT 2.0 Å, Cryo-EM structure of lysophosphatidylserine (18:0)-bound GPR174-Gs complex
- 6X18 2.1 Å, GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor
- 6X19 2.1 Å, Non peptide agonist CHU-128, bound to Glucagon-Like peptide-1 (GLP-1) Receptor
- 9NTU 2.1 Å, Cryo-EM structure of BETP-GLP-1(9-36)-GLP-1R-Gs complex
- 7RTB 2.14 Å, Peptide-19 bound to the Glucagon-Like Peptide-1 Receptor (GLP-1R)
Browse structure collections
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