Research workbench
Human TRIC/CCT complex with reovirus outer capsid protein sigma-3
Analyse Human TRIC/CCT complex with reovirus outer capsid protein sigma-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LUP
- Type
- protein
- Length
- 8,739 residues
- Chains
- 17
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-complex protein 1 subunit epsilon; T-complex protein 1 subunit beta; T-complex protein…
- UniProt
- P48643, P78371, P50991, P49368, Q99832, P50990, P40227, P17987, P03527
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 9 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, D | T-complex protein 1 subunit epsilon | protein | 527 | 48% helix, 14% strand | P48643 |
| M, E | T-complex protein 1 subunit beta | protein | 518 | 52% helix, 17% strand | P78371 |
| N, F | T-complex protein 1 subunit delta | protein | 518 | 49% helix, 18% strand | P50991 |
| H, P | T-complex protein 1 subunit gamma | protein | 521 | 48% helix, 14% strand | P49368 |
| K, C | T-complex protein 1 subunit eta | protein | 522 | 49% helix, 14% strand | Q99832 |
| J, B | T-complex protein 1 subunit theta | protein | 524 | 48% helix, 14% strand | P50990 |
| I, A | T-complex protein 1 subunit zeta | protein | 525 | 48% helix, 15% strand | P40227 |
| O, G | T-complex protein 1 subunit alpha | protein | 532 | 48% helix, 14% strand | P17987 |
| Q | Outer capsid protein sigma-3 | protein | 365 | 43% helix, 13% strand | P03527 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains Q
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1072 | 0.87 | 0.88 | 144 | empty |
| 2 | 1187 | 0.87 | 0.88 | 146 | empty |
| 3 | 1019 | 0.86 | 0.87 | 118 | empty |
| 4 | 870 | 0.85 | 0.88 | 124 | empty |
| 5 | 897 | 0.85 | 0.87 | 123 | empty |
Interfaces
54 interfaces between chains.
- H–G · 3633 Ų buried · 75 hydrogen bonds · protein-protein
- P–O · 3542 Ų buried · 74 hydrogen bonds · protein-protein
- L–M · 3519 Ų buried · 59 hydrogen bonds · protein-protein
- D–E · 3480 Ų buried · 53 hydrogen bonds · protein-protein
- D–C · 3445 Ų buried · 58 hydrogen bonds · protein-protein
Compared structures
- 7LUP · Human TRiC/CCT complex with reovirus outer capsid protein sigma-3 · 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 P48643
- Every structure of UniProt P78371
- Every structure of UniProt P50991
- Every structure of UniProt P49368
- Every structure of UniProt Q99832
- Every structure of UniProt P50990
- Every structure of UniProt P40227
- Every structure of UniProt P17987
- Every structure of UniProt P03527
- Elsewhere: RCSB PDB 7LUP · PDBe 7LUP · UniProt P48643 · UniProt P78371 · UniProt P50991 · UniProt P49368 · UniProt Q99832 · UniProt P50990 · UniProt P40227 · UniProt P17987 · UniProt P03527
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.