Research workbench
Structure of yeast npp-tric
Analyse Structure of yeast npp-tric in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GW4
- Type
- protein
- Length
- 8,446 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-complex protein 1 subunit alpha; T-complex protein 1 subunit beta; T-complex protein 1…
- UniProt
- P12612, P39076, P39078, P40413, P39077, P42943, P47079, P39079
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 8 distinct chains · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a, A | T-complex protein 1 subunit alpha | protein | 543 | 47% helix, 15% strand | P12612 |
| b, B | T-complex protein 1 subunit beta | protein | 517 | 49% helix, 15% strand | P39076 |
| d, D | T-complex protein 1 subunit delta | protein | 521 | 48% helix, 16% strand | P39078 |
| e, E | T-complex protein 1 subunit epsilon | protein | 528 | 50% helix, 13% strand | P40413 |
| g, G | T-complex protein 1 subunit gamma | protein | 518 | 48% helix, 9% strand | P39077 |
| h, H | T-complex protein 1 subunit eta | protein | 519 | 49% helix, 11% strand | P42943 |
| q, Q | T-complex protein 1 subunit theta | protein | 543 | 45% helix, 14% strand | P47079 |
| z, Z | T-complex protein 1 subunit zeta | protein | 534 | 51% helix, 11% strand | P39079 |
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 | 607 | 0.85 | 0.90 | 60 | empty |
| 2 | 1107 | 0.84 | 0.85 | 82 | empty |
| 3 | 931 | 0.84 | 0.86 | 80 | empty |
| 4 | 1136 | 0.84 | 0.85 | 105 | empty |
| 5 | 878 | 0.83 | 0.85 | 102 | empty |
Interfaces
36 interfaces between chains.
- b–e · 2336 Ų buried · 22 hydrogen bonds · protein-protein
- B–E · 2237 Ų buried · 33 hydrogen bonds · protein-protein
- Q–Z · 1868 Ų buried · 16 hydrogen bonds · protein-protein
- q–z · 1769 Ų buried · 15 hydrogen bonds · protein-protein
- A–G · 1511 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 5GW4 · Structure of Yeast NPP-TRiC · the same entry in another collection · chain Z against Z, 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 P12612
- Every structure of UniProt P39076
- Every structure of UniProt P39078
- Every structure of UniProt P40413
- Every structure of UniProt P39077
- Every structure of UniProt P42943
- Every structure of UniProt P47079
- Every structure of UniProt P39079
- Elsewhere: RCSB PDB 5GW4 · PDBe 5GW4 · UniProt P12612 · UniProt P39076 · UniProt P39078 · UniProt P40413 · UniProt P39077 · UniProt P42943 · UniProt P47079 · UniProt P39079
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