Research workbench
Model built against symmetry-free cryo-EM MAP of tric-ADP-alfx
Analyse Model built against symmetry-free cryo-EM MAP of tric-ADP-alfx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A0W
- Type
- protein
- Length
- 8,076 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-complex protein 1 subunit beta
- UniProt
- Q3ZBH0
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 6 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F, G, I, J, M, P | T-complex protein 1 subunit beta | protein | 513 | 48% helix, 13% strand | Q3ZBH0 |
| C | T-complex protein 1 subunit beta | protein | 490 | 48% helix, 13% strand | Q3ZBH0 |
| H | T-complex protein 1 subunit beta | protein | 492 | 48% helix, 12% strand | Q3ZBH0 |
| K | T-complex protein 1 subunit beta | protein | 491 | 48% helix, 11% strand | Q3ZBH0 |
| L, O | T-complex protein 1 subunit beta | protein | 490 | 48% helix, 11% strand | Q3ZBH0 |
| N | T-complex protein 1 subunit beta | protein | 493 | 48% helix, 10% strand | Q3ZBH0 |
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 | 905 | 0.89 | 0.92 | 147 | empty |
| 2 | 1147 | 0.87 | 0.88 | 144 | empty |
| 3 | 783 | 0.87 | 0.90 | 134 | empty |
| 4 | 1133 | 0.87 | 0.88 | 136 | empty |
| 5 | 1059 | 0.87 | 0.88 | 155 | empty |
Interfaces
32 interfaces between chains.
- B–F · 1355 Ų buried · 0 hydrogen bonds · protein-protein
- D–H · 1320 Ų buried · 4 hydrogen bonds · protein-protein
- B–G · 1233 Ų buried · 4 hydrogen bonds · protein-protein
- E–G · 1227 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 1147 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- Q3ZBH0 · AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit beta (Q3ZBH0) · a predicted model of the same protein · chain H against A, TM-score 0.85
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 Q3ZBH0
- Elsewhere: RCSB PDB 4A0W · PDBe 4A0W · UniProt Q3ZBH0
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