Research workbench
Model refined against the symmetry-free cryo-EM MAP of tric-AMP-pnp
Analyse Model refined against the symmetry-free cryo-EM MAP of tric-AMP-pnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A0V
- Type
- protein
- Length
- 7,959 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 0.90
Structure
electron microscopy · 9 distinct chains · 46% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-complex protein 1 subunit beta | protein | 492 | 47% helix, 11% strand | Q3ZBH0 |
| B, L | T-complex protein 1 subunit beta | protein | 484 | 46% helix, 11% strand | Q3ZBH0 |
| C, D, E, G, J, K, P | T-complex protein 1 subunit beta | protein | 513 | 45% helix, 12% strand | Q3ZBH0 |
| F | T-complex protein 1 subunit beta | protein | 489 | 46% helix, 13% strand | Q3ZBH0 |
| H | T-complex protein 1 subunit beta | protein | 485 | 45% helix, 11% strand | Q3ZBH0 |
| I | T-complex protein 1 subunit beta | protein | 476 | 45% helix, 11% strand | Q3ZBH0 |
| M | T-complex protein 1 subunit beta | protein | 486 | 47% helix, 10% strand | Q3ZBH0 |
| N | T-complex protein 1 subunit beta | protein | 490 | 48% helix, 13% strand | Q3ZBH0 |
| O | T-complex protein 1 subunit beta | protein | 482 | 46% 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 | 1084 | 0.90 | 0.92 | 165 | empty |
| 2 | 840 | 0.89 | 0.92 | 146 | empty |
| 3 | 1191 | 0.89 | 0.90 | 158 | empty |
| 4 | 944 | 0.89 | 0.90 | 140 | empty |
| 5 | 778 | 0.88 | 0.91 | 137 | empty |
Interfaces
33 interfaces between chains.
- B–F · 1534 Ų buried · 7 hydrogen bonds · protein-protein
- L–P · 1524 Ų buried · 13 hydrogen bonds · protein-protein
- E–G · 1289 Ų buried · 11 hydrogen bonds · protein-protein
- B–G · 1101 Ų buried · 14 hydrogen bonds · protein-protein
- A–F · 1100 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4A0V · model refined against the Symmetry-free cryo-EM map of TRiC-AMP-PNP · the same entry in another collection · chain J against J, 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 Q3ZBH0
- Elsewhere: RCSB PDB 4A0V · PDBe 4A0V · UniProt Q3ZBH0
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