Research workbench
Yeast tho-SUB2 complex dimer
Analyse Yeast tho-SUB2 complex dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AQO
- Type
- protein
- Length
- 5,611 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tho complex subunit 2; Tho complex subunit HPR1; TEX1 isoform 1…
- UniProt
- A0A6A5Q535, P17629, A0A6A5Q4V2, A0A6A5Q316, A0A6A5PZX4, P33441
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 8 distinct chains · 58% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, A | Tho complex subunit 2 | protein | 1079 | 65% helix, 3% strand | A0A6A5Q535 |
| H, B | Tho complex subunit HPR1 | protein | 563 | 57% helix, 0% strand | P17629 |
| K, E | TEX1 isoform 1 | protein | 348 | 7% helix, 39% strand | A0A6A5Q4V2 |
| L, F | EM14S01-3B_G0007820.MRNA.1.CDS.1 | protein | 361 | 42% helix, 17% strand | A0A6A5Q316 |
| J | BJ4_G0025130.MRNA.1.CDS.1 | protein | 230 | 77% helix, 1% strand | A0A6A5PZX4 |
| I | Tho complex subunit MFT1 | protein | 227 | 77% helix, 0% strand | P33441 |
| C | BJ4_G0025130.MRNA.1.CDS.1 | protein | 227 | 78% helix, 1% strand | A0A6A5PZX4 |
| D | Tho complex subunit MFT1 | protein | 225 | 76% helix, 0% strand | P33441 |
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 | 978 | 0.86 | 0.87 | 108 | empty |
| 2 | 1118 | 0.85 | 0.86 | 118 | empty |
| 3 | 1158 | 0.83 | 0.84 | 95 | empty |
| 4 | 990 | 0.83 | 0.84 | 80 | empty |
| 5 | 407 | 0.82 | 0.90 | 66 | empty |
Interfaces
25 interfaces between chains.
- A–B · 6627 Ų buried · 41 hydrogen bonds · protein-protein
- G–H · 6607 Ų buried · 41 hydrogen bonds · protein-protein
- J–I · 3731 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 3725 Ų buried · 18 hydrogen bonds · protein-protein
- H–J · 2463 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7AQO · yeast THO-Sub2 complex dimer · the same entry in another collection · chain D against D, 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 A0A6A5Q535
- Every structure of UniProt P17629
- Every structure of UniProt A0A6A5Q4V2
- Every structure of UniProt A0A6A5Q316
- Every structure of UniProt A0A6A5PZX4
- Every structure of UniProt P33441
- Elsewhere: RCSB PDB 7AQO · PDBe 7AQO · UniProt A0A6A5Q535 · UniProt P17629 · UniProt A0A6A5Q4V2 · UniProt A0A6A5Q316 · UniProt A0A6A5PZX4 · UniProt P33441
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