Research workbench
Double nuclear outer ring from the isolated yeast npc
Analyse Double nuclear outer ring from the isolated yeast npc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N84
- Type
- protein
- Length
- 10,313 residues
- Chains
- 17
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin NUP188; Unknown; Nucleoporin NUP120; Nucleoporin NUP85; Nucleoporin 145C…
- UniProt
- P52593, P35729, P46673, P49687, Q04491, P53011, P52891, P36161
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 13 distinct chains · 34% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Nucleoporin NUP188 | protein | 1137 | 41% helix, 0% strand | P52593 |
| Y, Z | Unknown | protein | 63 | 97% helix, 0% strand | — |
| a, l | Nucleoporin NUP120 | protein | 1006 | 26% helix, 15% strand | P35729 |
| b | Nucleoporin NUP85 | protein | 675 | 30% helix, 2% strand | P46673 |
| c | Nucleoporin 145C | protein | 559 | 42% helix, 3% strand | P49687 |
| d, o | Protein transport protein SEC13 | protein | 274 | 0% helix, 47% strand | Q04491 |
| e, p | Nucleoporin SEH1 | protein | 307 | 0% helix, 39% strand | P53011 |
| f | Nucleoporin NUP84 | protein | 649 | 48% helix, 0% strand | P52891 |
| g | Nucleoporin NUP133 | protein | 1062 | 27% helix, 10% strand | P36161 |
| m | Nucleoporin NUP85 | protein | 670 | 32% helix, 2% strand | P46673 |
| n | Nucleoporin 145C | protein | 557 | 49% helix, 2% strand | P49687 |
| q | Nucleoporin NUP84 | protein | 648 | 45% helix, 1% strand | P52891 |
| r | Nucleoporin NUP133 | protein | 1056 | 34% helix, 14% strand | P36161 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.87 | 0.93 | 62 | empty |
| 2 | 410 | 0.87 | 0.96 | 39 | empty |
| 3 | 602 | 0.85 | 0.90 | 55 | empty |
| 4 | 736 | 0.83 | 0.86 | 57 | empty |
| 5 | 145 | 0.81 | 0.97 | 23 | empty |
Interfaces
27 interfaces between chains.
- m–p · 4280 Ų buried · 45 hydrogen bonds · protein-protein
- b–e · 4024 Ų buried · 38 hydrogen bonds · protein-protein
- c–d · 3589 Ų buried · 36 hydrogen bonds · protein-protein
- n–o · 3290 Ų buried · 26 hydrogen bonds · protein-protein
- X–q · 3017 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 7N84 · Double nuclear outer ring from the isolated yeast NPC · the same entry in another collection · chain l against l, TM-score 1.00
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 P52593
- Every structure of UniProt P35729
- Every structure of UniProt P46673
- Every structure of UniProt P49687
- Every structure of UniProt Q04491
- Every structure of UniProt P53011
- Every structure of UniProt P52891
- Every structure of UniProt P36161
- Elsewhere: RCSB PDB 7N84 · PDBe 7N84 · UniProt P52593 · UniProt P35729 · UniProt P46673 · UniProt P49687 · UniProt Q04491 · UniProt P53011 · UniProt P52891 · UniProt P36161
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