8XGM: Human GPR1
Cryo-EM structure of human GPR1 bound to chemerin. Determined by electron microscopy at 3.29 Å resolution. Released 21 Aug 2024.
- Method
- Electron microscopy
- Resolution
- 3.29 Å
- Organisms
- Vicugna pacos, Homo sapiens
- Chains
- 6
- Atoms
- 10,319
- Mol. weight
- 162.36 kDa
- Ligands
- CLR
- Released
- 21 Aug 2024
Explore 8XGM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8XGM contains 38 α-helices and 75 β-strands across 6 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: 17 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 25-26 | 2 | 6 |
| α-helix | 36-60 | 25 | |
| α-helix | 61-65 | 5 | |
| α-helix | 71-88 | 18 | |
| α-helix | 90-98 | 9 | |
| α-helix | 107-140 | 34 | |
| α-helix | 142-146 | 5 | |
| α-helix | 151-169 | 19 | |
| α-helix | 172-175 | 4 | |
| β-strand | 176-180 | 5 | 7 |
| β-strand | 185-189 | 5 | 7 |
| α-helix | 199-211 | 13 | |
| α-helix | 212-216 | 5 | |
| α-helix | 217-236 | 20 | |
| α-helix | 249-268 | 20 | |
| α-helix | 269-272 | 4 | |
| α-helix | 280-283 | 4 | |
| α-helix | 286-301 | 16 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-317 | 9 | |
Chain B: 3 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-24 | 21 | |
| α-helix | 30-32 | 3 | |
| β-strand | 47-51 | 5 | 8 |
| β-strand | 58-63 | 6 | 9 |
| β-strand | 69-74 | 6 | 9 |
| β-strand | 78-83 | 6 | 9 |
| β-strand | 89-94 | 6 | 9 |
| β-strand | 100-105 | 6 | 10 |
| β-strand | 111-116 | 6 | 10 |
| β-strand | 120-125 | 6 | 10 |
| β-strand | 135-140 | 6 | 10 |
| β-strand | 146-151 | 6 | 11 |
| β-strand | 157-161 | 5 | 11 |
| β-strand | 165-168 | 4 | 11 |
| β-strand | 178-181 | 4 | 11 |
| β-strand | 187 | 1 | 12 |
| β-strand | 191-192 | 2 | 13 |
| β-strand | 198-202 | 5 | 13 |
| β-strand | 203 | 1 | 12 |
| β-strand | 207-212 | 6 | 13 |
| β-strand | 218-223 | 6 | 13 |
| β-strand | 229-234 | 6 | 14 |
| β-strand | 240-245 | 6 | 14 |
| β-strand | 250-254 | 5 | 14 |
| β-strand | 260-264 | 5 | 14 |
| β-strand | 273-278 | 6 | 15 |
| α-helix | 280-282 | 3 | |
| β-strand | 284-289 | 6 | 15 |
| β-strand | 294-298 | 5 | 15 |
| β-strand | 304-308 | 5 | 15 |
| β-strand | 315-320 | 6 | 8 |
| β-strand | 327-332 | 6 | 8 |
| β-strand | 334-339 | 6 | 8 |
Chain C: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-29 | 23 | |
| β-strand | 34-40 | 7 | 16 |
| α-helix | 46-52 | 7 | |
| β-strand | 184-191 | 8 | 16 |
| β-strand | 194-201 | 8 | 16 |
| β-strand | 220-226 | 7 | 16 |
| β-strand | 233 | 1 | 17 |
| α-helix | 234 | 1 | |
| β-strand | 241 | 1 | 17 |
| α-helix | 242-253 | 12 | |
| β-strand | 263-269 | 7 | 16 |
| α-helix | 271-278 | 8 | |
| α-helix | 300-308 | 9 | |
| β-strand | 319 | 1 | 16 |
| β-strand | 322-323 | 2 | 16 |
| α-helix | 330-350 | 21 | |
Chain D: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| β-strand | 27-40 | 14 | 6 |
| β-strand | 43-54 | 12 | 6 |
| β-strand | 55 | 1 | 18 |
| α-helix | 67-68 | 2 | |
| β-strand | 69 | 1 | 18 |
| β-strand | 75-84 | 10 | 6 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-96 | 7 | 6 |
| α-helix | 106-119 | 14 | |
| β-strand | 121 | 1 | 19 |
| β-strand | 124 | 1 | 19 |
Chain G: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-22 | 14 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 54-55 | 2 | |
Chain S: 3 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 17-24 | 8 | 1 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 65 | 1 | 1 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-84 | 7 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 110-111 | 2 | 2 |
| β-strand | 115-119 | 5 | 2 |
| α-helix | 137-139 | 3 | |
| β-strand | 140-141 | 2 | 3 |
| β-strand | 146-148 | 3 | 4 |
| β-strand | 155-161 | 7 | 3 |
| β-strand | 166 | 1 | 5 |
| β-strand | 172 | 1 | 5 |
| β-strand | 174-179 | 6 | 4 |
| β-strand | 186-190 | 5 | 4 |
| β-strand | 194-195 | 2 | 4 |
| α-helix | 196 | 1 | |
| β-strand | 203-208 | 6 | 3 |
| β-strand | 211-216 | 6 | 3 |
| β-strand | 225-231 | 7 | 4 |
| β-strand | 239 | 1 | 4 |
| β-strand | 243-246 | 4 | 4 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| scFV16 | S | protein | 247 | Vicugna pacos | |
| G-protein coupled receptor 1 | A | protein | 306 | Homo sapiens | P46091 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 340 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(i) subunit alpha-1 | C | protein | 354 | Homo sapiens | P63096 (AlphaFold model) |
| Guanine nucleotide-binding protein subunit gamma | G | protein | 55 | Homo sapiens | P59768 (AlphaFold model) |
| Retinoic acid receptor responder protein 2 | D | protein | 137 | Homo sapiens | Q99969 |
Sequence of entity 1 (S), FASTA
>8XGM_1 scFV16 (chains S)
DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY
ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS
SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR
PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG
AGTKLEL
Sequence of entity 2 (A), FASTA
>8XGM_2 G-protein coupled receptor 1 (chains A)
NYSYDLDYYSLESDLEEKVQLGVVHWVSLVLYCLAFVLGIPGNAIVIWFTGFKWKKTVTT
LWFLNLAIADFIFLLFLPLYISYVAMNFHWPFGIWLCKANSFTAQLNMFASVFFLTVISL
DHYIHLIHPVLSHRHRTLKNSLIVIIFIWLLASLIGGPALYFRDTVEFNNHTLCYNNFQK
HDPDLTLIRHHVLTWVKFIIGYLFPLLTMSICYLCLIFKVKKRSILISSRHFWTILVVVV
AFVVCWTPYHLFSIWELTIHHNSYSHHVMQAGIPLSTGLAFLNSCLNPILYVLISKKFQA
RFRSSV
Sequence of entity 3 (B), FASTA
>8XGM_3 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 4 (C), FASTA
>8XGM_4 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains C)
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVGAQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA
AYIQCQFEDLNKRKDTKEIYTHFTCSTDTKNVQFVFDAVTDVIIKNNLKDCGLF
Sequence of entity 5 (G), FASTA
>8XGM_5 Guanine nucleotide-binding protein subunit gamma (chains G)
SIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFR
Sequence of entity 6 (D), FASTA
>8XGM_6 Retinoic acid receptor responder protein 2 (chains D)
ELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKR
DWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQR
AGEDPHSFYFPGQFAFS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CLR | Cholesterol | C27 H46 O | 1 |
Primary citation
Structure of G protein-coupled receptor GPR1 bound to full-length chemerin adipokine reveals a chemokine-like reverse binding mode. Liu, A., Liu, Y., Chen, G. et al. PLoS Biol (2024) 22:e3002838-e3002838. DOI 10.1371/journal.pbio.3002838 · PubMed
Other PDB entries of the same protein (UniProt P46091 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8JJP 2.9 Å, G protein-coupled receptor 1
- 9UYN 2.9 Å, Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to beta-arrestin 1 in…
- 9UYI 3.2 Å, Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and…
- 9UYH 3.3 Å, Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and…
- 9UYJ 3.3 Å, Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and…
- 9UYL 3.3 Å, Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and…
- 9UYM 3.5 Å, Composite map of the G protein-coupled receptor 1 (GPR1) bound to chemerin and…
- 9L3Y 3.6 Å, Cryo-EM structure of the G-protein coupled receptor 1 (GPR1) in complex with chemerin…
Browse structure collections
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