Research workbench
Crystal structure of the NUP85/SEH1 complex
Analyse Crystal structure of the NUP85/SEH1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EWE
- Type
- protein
- Length
- 1,300 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin SEH1; Nucleoporin NUP85
- UniProt
- P53011, P46673
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Nucleoporin SEH1 | protein | 255 | 0% helix, 47% strand | P53011 |
| B, D | Nucleoporin NUP85 | protein | 395 | 67% helix, 2% strand | P46673 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 775 | 0.85 | 0.88 | 62 | empty |
| 2 | 516 | 0.83 | 0.89 | 49 | empty |
| 3 | 581 | 0.83 | 0.88 | 76 | empty |
| 4 | 238 | 0.78 | 0.91 | 42 | empty |
| 5 | 138 | 0.68 | 0.89 | 34 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1721 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1669 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 606 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 584 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 233 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3EWE · Crystal Structure of the Nup85/Seh1 Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P46673 · AlphaFold monomer V2.0 prediction for nucleoporin NUP85 (P46673) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P53011 · AlphaFold monomer V2.0 prediction for nucleoporin SEH1 (P53011) · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P53011
- Every structure of UniProt P46673
- Elsewhere: RCSB PDB 3EWE · PDBe 3EWE · UniProt P53011 · UniProt P46673
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