5NVK: Human 4EHP-GIGYF1 complex
Crystal structure of the human 4EHP-GIGYF1 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 26 Jul 2017.
- Method
- X-ray diffraction
- Resolution
- 2.9 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,833
- Mol. weight
- 122.85 kDa
- Released
- 26 Jul 2017
Explore 5NVK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5NVK contains 54 α-helices and 44 β-strands across 8 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: 6 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 53 | 1 | 1 |
| β-strand | 55-66 | 12 | 2 |
| β-strand | 83-90 | 8 | 2 |
| α-helix | 91-98 | 8 | |
| β-strand | 101 | 1 | 3 |
| α-helix | 104-106 | 3 | |
| β-strand | 111-117 | 7 | 2 |
| β-strand | 133-139 | 7 | 2 |
| α-helix | 144-156 | 13 | |
| β-strand | 166-173 | 8 | 2 |
| β-strand | 178-184 | 7 | 2 |
| α-helix | 190-204 | 15 | |
| α-helix | 206-207 | 2 | |
| β-strand | 213-216 | 4 | 2 |
| α-helix | 217-220 | 4 | |
Chains B and H: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-48 | 6 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-61 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 69 | 1 | 3 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 84-92 | 9 | |
| β-strand | 95 | 1 | 2 |
| α-helix | 97-100 | 4 | |
Chain C: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 55-66 | 12 | 4 |
| β-strand | 83-90 | 8 | 4 |
| α-helix | 91-98 | 8 | |
| β-strand | 101 | 1 | 5 |
| α-helix | 104-106 | 3 | |
| β-strand | 111-117 | 7 | 4 |
| β-strand | 133-139 | 7 | 4 |
| α-helix | 144-156 | 13 | |
| β-strand | 166-173 | 8 | 4 |
| β-strand | 178-184 | 7 | 4 |
| α-helix | 190-203 | 14 | |
| β-strand | 213-216 | 4 | 4 |
Chain D: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32 | 1 | 1 |
| α-helix | 43-48 | 6 | |
| α-helix | 59-61 | 3 | |
| α-helix | 63-65 | 3 | |
| β-strand | 69 | 1 | 5 |
| α-helix | 73-76 | 4 | |
| α-helix | 77-79 | 3 | |
| α-helix | 84-89 | 6 | |
| β-strand | 95 | 1 | 4 |
| α-helix | 97-100 | 4 | |
Chain E: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 55-66 | 12 | 6 |
| α-helix | 67-69 | 3 | |
| α-helix | 75-80 | 6 | |
| β-strand | 83-90 | 8 | 6 |
| α-helix | 91-98 | 8 | |
| β-strand | 101 | 1 | 7 |
| α-helix | 102-103 | 2 | |
| α-helix | 104-106 | 3 | |
| β-strand | 111-117 | 7 | 6 |
| α-helix | 127-130 | 4 | |
| β-strand | 133-139 | 7 | 6 |
| α-helix | 144-156 | 13 | |
| β-strand | 166-173 | 8 | 6 |
| β-strand | 178-184 | 7 | 6 |
| α-helix | 190-204 | 15 | |
| β-strand | 213-216 | 4 | 6 |
Chain F: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-48 | 6 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-61 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 69 | 1 | 7 |
| α-helix | 77-79 | 3 | |
| α-helix | 84-90 | 7 | |
| β-strand | 95 | 1 | 6 |
| α-helix | 97-100 | 4 | |
Chain G: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 55-66 | 12 | 8 |
| β-strand | 82-90 | 9 | 8 |
| α-helix | 91-98 | 8 | |
| β-strand | 101 | 1 | 9 |
| α-helix | 104-106 | 3 | |
| β-strand | 111-117 | 7 | 8 |
| β-strand | 133-139 | 7 | 8 |
| α-helix | 144-156 | 13 | |
| β-strand | 166-173 | 8 | 8 |
| β-strand | 178-184 | 7 | 8 |
| α-helix | 190-204 | 15 | |
| α-helix | 206-207 | 2 | |
| β-strand | 213-216 | 4 | 8 |
| α-helix | 217-220 | 4 | |
| β-strand | 223 | 1 | 10 |
| β-strand | 226 | 1 | 10 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Eukaryotic translation initiation factor 4E type 2 | A, C, E, G | protein | 189 | Homo sapiens | O60573 (AlphaFold model) |
| GRB10-interacting GYF protein 1 | B, D, F, H | protein | 75 | Homo sapiens | O75420 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>5NVK_1 Eukaryotic translation initiation factor 4E type 2 (chains A, C, E, G)
GPHMLEAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPG
DLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEE
ICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPG
RLGPQRLLF
Sequence of entity 2 (B, D, F, H), FASTA
>5NVK_2 GRB10-interacting GYF protein 1 (chains B, D, F, H)
GPHMKYKLADYRYGREEMLALYVKENKVPEELQDKEFAAVLQDEPLQPLALEPLTEEEQR
NFSLSVNSVAVLRLM
Primary citation
GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression. Peter, D., Weber, R., Sandmeir, F. et al. Genes Dev (2017) 31:1147-1161. DOI 10.1101/gad.299420.117 · PubMed
Other PDB entries of the same protein (UniProt O60573 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2JGB 1.7 Å, Structure of human eIF4E homologous protein 4EHP with m7GTP
- 5NVN 1.9 Å, Crystal structure of the human 4EHP-4E-BP1 complex
- 5XLN 1.9 Å, Crystal structure of the TRS_UNE-T and 4EHP complex
- 5NVM 2.0 Å, Crystal structure of the human 4EHP-GIGYF2 complex lacking the auxiliary sequences
- 5NVL 2.3 Å, Crystal structure of the human 4EHP-GIGYF2 complex
- 2JGC 2.4 Å, Structure of the human eIF4E homologous protein, 4EHP without ligand bound
Browse structure collections
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