Research workbench
The rhodococcus 20S proteasome
Analyse The rhodococcus 20S proteasome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q5Q
- Type
- protein
- Length
- 3,101 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome alpha-type subunit 1; Proteasome beta-type subunit 1
- EC
- 3.4.25.1
- UniProt
- Q53080, Q53079
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Proteasome alpha-type subunit 1 (EC 3.4.25.1) | protein | 219 | 39% helix, 24% strand | Q53080 |
| H, I, J, K, L, M, N | Proteasome beta-type subunit 1 | protein | 224 | 38% helix, 28% strand | Q53079 |
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 | 1133 | 0.78 | 0.80 | 137 | empty |
| 2 | 1011 | 0.77 | 0.79 | 112 | empty |
| 3 | 1088 | 0.77 | 0.79 | 122 | empty |
| 4 | 1044 | 0.76 | 0.79 | 125 | empty |
| 5 | 812 | 0.75 | 0.79 | 88 | empty |
Interfaces
28 interfaces between chains.
- A–G · 776 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 773 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 767 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 766 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 759 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1Q5Q · The Rhodococcus 20S proteasome · the same entry in another collection · chain N against N, 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 Q53080
- Every structure of UniProt Q53079
- Elsewhere: RCSB PDB 1Q5Q · PDBe 1Q5Q · UniProt Q53080 · UniProt Q53079
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