9NEM: Unc119-Farnesylated peptide complex
Structure of Unc119-Farnesylated peptide complex. Determined by X-ray diffraction at 2.49 Å resolution. Released 3 Sept 2025.
- Method
- X-ray diffraction
- Resolution
- 2.49 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 8,490
- Mol. weight
- 139.18 kDa
- Ligands
- FAR
- Released
- 3 Sept 2025
Explore 9NEM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9NEM contains 33 α-helices and 56 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: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-64 | 4 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 1 |
| β-strand | 100-105 | 6 | 1 |
| β-strand | 127-131 | 5 | 2 |
| α-helix | 134-138 | 5 | |
| β-strand | 141-149 | 9 | 1 |
| β-strand | 158-166 | 9 | 2 |
| β-strand | 169-177 | 9 | 2 |
| α-helix | 180-182 | 3 | |
| β-strand | 186-194 | 9 | 1 |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 2 |
| β-strand | 225-234 | 10 | 2 |
Chain B: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-63 | 3 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 3 |
| β-strand | 100-105 | 6 | 3 |
| β-strand | 127-131 | 5 | 4 |
| α-helix | 134-138 | 5 | |
| β-strand | 141-149 | 9 | 3 |
| β-strand | 158-166 | 9 | 4 |
| β-strand | 169-177 | 9 | 4 |
| β-strand | 186-194 | 9 | 3 |
| α-helix | 195-199 | 5 | |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 4 |
| β-strand | 224-234 | 11 | 4 |
Chain C: 6 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-63 | 3 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 5 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 127-131 | 5 | 6 |
| α-helix | 134-138 | 5 | |
| β-strand | 141-149 | 9 | 5 |
| β-strand | 159-166 | 8 | 6 |
| β-strand | 170-177 | 8 | 6 |
| α-helix | 180-182 | 3 | |
| β-strand | 186-194 | 9 | 5 |
| α-helix | 195-197 | 3 | |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 6 |
| β-strand | 224-234 | 11 | 6 |
Chain D: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-65 | 5 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 7 |
| β-strand | 100-105 | 6 | 7 |
| β-strand | 127-131 | 5 | 8 |
| α-helix | 134-138 | 5 | |
| β-strand | 141-149 | 9 | 7 |
| β-strand | 159-166 | 8 | 8 |
| β-strand | 169-177 | 9 | 8 |
| β-strand | 186-194 | 9 | 7 |
| α-helix | 195-197 | 3 | |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 8 |
| β-strand | 224-234 | 11 | 8 |
Chain E: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-63 | 3 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 9 |
| β-strand | 100-104 | 5 | 9 |
| β-strand | 127-132 | 6 | 10 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-149 | 9 | 9 |
| β-strand | 158-166 | 9 | 10 |
| β-strand | 170-177 | 8 | 10 |
| β-strand | 186-194 | 9 | 9 |
| α-helix | 195-197 | 3 | |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 10 |
| β-strand | 224-235 | 12 | 10 |
Chain F: 7 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 61-63 | 3 | |
| α-helix | 78-80 | 3 | |
| β-strand | 86-94 | 9 | 11 |
| β-strand | 100-103 | 4 | 11 |
| β-strand | 127-131 | 5 | 12 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-149 | 9 | 11 |
| β-strand | 155 | 1 | 13 |
| β-strand | 158-166 | 9 | 12 |
| β-strand | 169-177 | 9 | 12 |
| α-helix | 180 | 1 | |
| β-strand | 181 | 1 | 13 |
| α-helix | 182 | 1 | |
| β-strand | 186-194 | 9 | 11 |
| α-helix | 195-196 | 2 | |
| α-helix | 200-208 | 9 | |
| β-strand | 213-221 | 9 | 12 |
| β-strand | 224-234 | 11 | 12 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein unc-119 homolog A | A, B, C, D, E, F | protein | 196 | Homo sapiens | Q13432 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>9NEM_1 Protein unc-119 homolog A (chains A, B, C, D, E, F)
MGSSHHHHHHSSKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFE
IKKPPVSERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIER
HYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDD
RLVMHNKADYSYSGTP
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| FAR | Farnesyl | C15 H26 | 5 |
Primary citation
Inhibition of Unc119b improves insulin sensitivity through potentiation of Rac1 activation in skeletal muscle and brown adipose tissue. Mittal, A., Buscaglia, P., Srivastava, D. et al. Mol Metab (2025) 100:102230-102230. DOI 10.1016/j.molmet.2025.102230 · PubMed
Other PDB entries of the same protein (UniProt Q13432 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3GQQ 1.95 Å, Crystal structure of the human retinal protein 4 (unc-119 homolog A). Northeast…
- 3RBQ 2.0 Å, Co-crystal structure of human UNC119 (retina gene 4) and an N-terminal Transducin-alpha…
- 6H6A 2.0 Å, Crystal structure of UNC119 in complex with LCK peptide
- 4GOJ 2.1 Å, The Crystal Structure of full length Arl3GppNHp in complex with UNC119a
- 5L7K 2.1 Å, The crystal structure of myristoylated NPHP3 peptide in complex with UNC119a
- 9GKG 2.21 Å, Crystal structure of UNC119 in complex with Squarunkin A
- 7UMO 2.3 Å, Structure of Unc119-inhibitor complex.
- 4GOK 2.6 Å, The Crystal structure of Arl2GppNHp in complex with UNC119a
Browse structure collections
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