Research workbench
Structural basis of cullin-2 ring E3 ligase regulation by the COP9 signalosome
Analyse Structural basis of cullin-2 ring E3 ligase regulation by the COP9 signalosome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R7H
- Type
- protein
- Length
- 3,592 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COP9 signalosome complex subunit 1; Elongin-C; Cullin-2; E3 ubiquitin-protein ligase…
- EC
- 3.4.-.-
- UniProt
- Q13098, Q15369, Q13617, P61201, Q9UNS2, Q9BT78, Q92905, Q7L5N1, Q9H9Q2, Q99627, Q15370
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 12 distinct chains · 52% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | COP9 signalosome complex subunit 1 | protein | 433 | 58% helix, 2% strand | Q13098 |
| Q | Elongin-C | protein | 112 | 32% helix, 11% strand | Q15369 |
| O | Cullin-2 | protein | 654 | 57% helix, 3% strand | Q13617 |
| R | E3 ubiquitin-protein ligase RBX1 | protein | 90 | 8% helix, 8% strand | — |
| B | COP9 signalosome complex subunit 2 | protein | 414 | 60% helix, 2% strand | P61201 |
| C | COP9 signalosome complex subunit 3 | protein | 403 | 55% helix, 3% strand | Q9UNS2 |
| D | COP9 signalosome complex subunit 4 | protein | 406 | 68% helix, 2% strand | Q9BT78 |
| E | COP9 signalosome complex subunit 5 (EC 3.4.-.-) | protein | 311 | 37% helix, 14% strand | Q92905 |
| F | COP9 signalosome complex subunit 6 | protein | 288 | 40% helix, 19% strand | Q7L5N1 |
| G | COP9 signalosome complex subunit 7B | protein | 208 | 51% helix, 6% strand | Q9H9Q2 |
| H | COP9 signalosome complex subunit 8 | protein | 169 | 60% helix, 5% strand | Q99627 |
| P | Elongin-B | protein | 104 | 15% helix, 26% strand | Q15370 |
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 | 1074 | 0.86 | 0.87 | 118 | empty |
| 2 | 329 | 0.83 | 0.93 | 45 | empty |
| 3 | 977 | 0.75 | 0.78 | 67 | empty |
| 4 | 68 | 0.74 | 0.98 | 19 | empty |
| 5 | 82 | 0.72 | 0.95 | 23 | empty |
Interfaces
30 interfaces between chains.
- E–F · 3775 Ų buried · 14 hydrogen bonds · protein-protein
- O–R · 2444 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 2423 Ų buried · 19 hydrogen bonds · protein-protein
- O–B · 2331 Ų buried · 28 hydrogen bonds · protein-protein
- F–G · 2144 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6R7H · Structural basis of Cullin-2 RING E3 ligase regulation by the COP9 signalosome · 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 Q13098
- Every structure of UniProt Q15369
- Every structure of UniProt Q13617
- Every structure of UniProt P61201
- Every structure of UniProt Q9UNS2
- Every structure of UniProt Q9BT78
- Every structure of UniProt Q92905
- Every structure of UniProt Q7L5N1
- Every structure of UniProt Q9H9Q2
- Every structure of UniProt Q99627
- Every structure of UniProt Q15370
- Elsewhere: RCSB PDB 6R7H · PDBe 6R7H · UniProt Q13098 · UniProt Q15369 · UniProt Q13617 · UniProt P61201 · UniProt Q9UNS2 · UniProt Q9BT78 · UniProt Q92905 · UniProt Q7L5N1 · UniProt Q9H9Q2 · UniProt Q99627 · UniProt Q15370
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