4DHX: ENY2:GANP complex
ENY2:GANP complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Jun 2012.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 4,306
- Mol. weight
- 63.32 kDa
- Released
- 13 Jun 2012
Explore 4DHX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4DHX contains 23 α-helices and 0 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: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1167-1231 | 65 | |
Chain B: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-22 | 13 | |
| α-helix | 25-39 | 15 | |
| α-helix | 42-57 | 16 | |
| α-helix | 64-78 | 15 | |
| α-helix | 81-98 | 18 | |
Chain C: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-22 | 15 | |
| α-helix | 25-39 | 15 | |
| α-helix | 42-57 | 16 | |
| α-helix | 64-77 | 14 | |
| α-helix | 81-96 | 16 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1167-1233 | 67 | |
Chain E: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-23 | 14 | |
| α-helix | 25-39 | 15 | |
| α-helix | 42-57 | 16 | |
| α-helix | 64-77 | 14 | |
| α-helix | 81-98 | 18 | |
Chain F: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-23 | 14 | |
| α-helix | 25-39 | 15 | |
| α-helix | 42-57 | 16 | |
| α-helix | 59-61 | 3 | |
| α-helix | 64-77 | 14 | |
| α-helix | 81-96 | 16 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 80 kDa MCM3-associated protein | A, D | protein | 75 | Homo sapiens | O60318 (AlphaFold model) |
| Enhancer of yellow 2 transcription factor homolog | B, C, E, F | protein | 101 | Homo sapiens | Q9NPA8 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>4DHX_1 80 kDa MCM3-associated protein (chains A, D)
GSLVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETDQRVRVARCCEDVCAHLVDLF
LVEEIFQTAKETLQE
Sequence of entity 2 (B, C, E, F), FASTA
>4DHX_2 Enhancer of yellow 2 transcription factor homolog (chains B, C, E, F)
MVVSKMNKDAQMRAAINQKLIETGERERLKELLRAKLIECGWKDQLKAHCKEVIKEKGLE
HVTVDDLVAEITPKGRALVPDSVKKELLQRIRTFLAQHASL
Primary citation
Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export. Jani, D., Lutz, S., Hurt, E. et al. Nucleic Acids Res (2012) 40:4562-4573. DOI 10.1093/nar/gks059 · PubMed
Other PDB entries of the same protein (UniProt O60318 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9DLP 2.79 Å, Cryo-EM structure of human TREX-2 complex bound to DDX39B(UAP56)
- 9T6N 3.0 Å, Cryo-EM structure of the human GANP-PCID2-DSS1 complex bound to UAP56
- 9UPC 3.14 Å, Structure of human TREX-2
- 9UPB 3.41 Å, Structure of the human TREX-2 bound to UAP56
- 8R7J 3.5 Å, Cryo-EM structure of the human TREX-2 complex
- 8R7K 3.5 Å, Cryo-EM structure of the human UAP56 - TREX-2 complex
Browse structure collections
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