Research workbench
Structure of the yeast coat nucleoporin complex, space group P212121
Analyse Structure of the yeast coat nucleoporin complex, space group P212121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XMN
- Type
- protein
- Length
- 2,659 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q04491, P49687, P52891, P35729, P46673
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 274 | — | Q04491 |
| B | — | protein | 503 | — | P49687 |
| F | — | protein | 419 | — | P52891 |
| E | — | protein | 896 | — | P35729 |
| D | — | protein | 143 | — | P46673 |
| L | — | protein | 209 | — | — |
| H | — | protein | 215 | — | — |
Compared structures
- 4XMN · Structure of the yeast coat nucleoporin complex, space group P212121 · the same entry in another collection · chain H against H, TM-score 1.00
- P52891 · AlphaFold monomer V2.0 prediction for nucleoporin NUP84 (P52891) · a predicted model of the same protein · chain F against A, TM-score 0.99
- Q04491 · AlphaFold monomer V2.0 prediction for protein transport protein SEC13 (Q04491) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P49687 · AlphaFold monomer V2.0 prediction for nucleoporin NUP145 (P49687) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P35729 · AlphaFold monomer V2.0 prediction for nucleoporin NUP120 (P35729) · a predicted model of the same protein · chain E against A, TM-score 0.96
- P46673 · AlphaFold monomer V2.0 prediction for nucleoporin NUP85 (P46673) · a predicted model of the same protein · chain D against A, TM-score 0.72
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 Q04491
- Every structure of UniProt P49687
- Every structure of UniProt P52891
- Every structure of UniProt P35729
- Every structure of UniProt P46673
- Elsewhere: RCSB PDB 4XMN · PDBe 4XMN · UniProt Q04491 · UniProt P49687 · UniProt P52891 · UniProt P35729 · UniProt P46673
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