Research workbench
Single particle cryo-EM structure of the chaetomium thermophilum NUP192-NIC96 complex (NUP192 residues 1-1756; NIC96 residues 240-301)
Analyse Single particle cryo-EM structure of the chaetomium thermophilum NUP192-NIC96… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MVU
- Type
- protein
- Length
- 1,604 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin NUP192; Nucleoporin NIC96
- UniProt
- G0S4T0, G0S024
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin NUP192 | protein | 1541 | 67% helix, 1% strand | G0S4T0 |
| B | Nucleoporin NIC96 | protein | 63 | 71% helix, 0% strand | G0S024 |
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 | 271 | 0.79 | 0.90 | 55 | empty |
| 2 | 110 | 0.77 | 0.96 | 25 | empty |
| 3 | 661 | 0.75 | 0.81 | 70 | empty |
| 4 | 202 | 0.75 | 0.89 | 35 | empty |
| 5 | 52 | 0.68 | 0.95 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1896 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7MVU · Single particle cryo-EM structure of the Chaetomium thermophilum Nup192-Nic96 complex… · the same entry in another collection · chain A against A, TM-score 1.00
- G0S4T0 · AlphaFold monomer V2.0 prediction for nucleoporin NUP192 (G0S4T0) · a predicted model of the same protein · chain A against A, TM-score 0.89
- G0S024 · AlphaFold monomer V2.0 prediction for nucleoporin NIC96 (G0S024) · a predicted model of the same protein · chain B against A, TM-score 0.59
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 G0S4T0
- Every structure of UniProt G0S024
- Elsewhere: RCSB PDB 7MVU · PDBe 7MVU · UniProt G0S4T0 · UniProt G0S024
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