Research workbench
Model refined against symmetry-free cryo-EM MAP of tric-ADP
Analyse Model refined against symmetry-free cryo-EM MAP of tric-ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A13
- Type
- protein
- Length
- 7,990 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 · 8 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F, I, M, O | T-complex protein 1 subunit beta | protein | 513 | 48% helix, 11% strand | Q3ZBH0 |
| B, N | T-complex protein 1 subunit beta | protein | 488 | 49% helix, 13% strand | Q3ZBH0 |
| D, H | T-complex protein 1 subunit beta | protein | 489 | 50% helix, 12% strand | Q3ZBH0 |
| G | T-complex protein 1 subunit beta | protein | 487 | 49% helix, 12% strand | Q3ZBH0 |
| J | T-complex protein 1 subunit beta | protein | 485 | 45% helix, 13% strand | Q3ZBH0 |
| K | T-complex protein 1 subunit beta | protein | 490 | 48% helix, 13% strand | Q3ZBH0 |
| L | T-complex protein 1 subunit beta | protein | 494 | 48% helix, 11% strand | Q3ZBH0 |
| P | T-complex protein 1 subunit beta | protein | 489 | 50% helix, 13% 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 | 1073 | 0.90 | 0.91 | 164 | empty |
| 2 | 1135 | 0.88 | 0.89 | 132 | empty |
| 3 | 610 | 0.87 | 0.92 | 96 | empty |
| 4 | 1172 | 0.87 | 0.88 | 108 | empty |
| 5 | 1077 | 0.87 | 0.88 | 98 | empty |
Interfaces
38 interfaces between chains.
- L–P · 1855 Ų buried · 13 hydrogen bonds · protein-protein
- B–G · 1703 Ų buried · 9 hydrogen bonds · protein-protein
- J–N · 1602 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 1595 Ų buried · 10 hydrogen bonds · protein-protein
- I–O · 1582 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4A13 · model refined against symmetry-free cryo-EM map of TRiC-ADP · the same entry in another collection · chain P against P, 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 4A13 · PDBe 4A13 · UniProt Q3ZBH0
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