Research workbench
Mouse PA28BETA
Analyse Mouse PA28BETA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MSK
- Type
- protein
- Length
- 1,451 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome activator complex subunit 2
- UniProt
- P97372
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 7 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome activator complex subunit 2 | protein | 210 | 75% helix, 1% strand | P97372 |
| B | Proteasome activator complex subunit 2 | protein | 211 | 75% helix, 1% strand | P97372 |
| C | Proteasome activator complex subunit 2 | protein | 206 | 76% helix, 1% strand | P97372 |
| D | Proteasome activator complex subunit 2 | protein | 207 | 76% helix, 1% strand | P97372 |
| E | Proteasome activator complex subunit 2 | protein | 201 | 76% helix, 1% strand | P97372 |
| F | Proteasome activator complex subunit 2 | protein | 208 | 76% helix, 1% strand | P97372 |
| G | Proteasome activator complex subunit 2 | protein | 208 | 75% helix, 1% strand | P97372 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.72 | 0.81 | 60 | empty |
| 2 | 512 | 0.70 | 0.80 | 59 | empty |
| 3 | 500 | 0.70 | 0.80 | 62 | empty |
| 4 | 488 | 0.70 | 0.80 | 64 | empty |
| 5 | 487 | 0.70 | 0.80 | 62 | empty |
Interfaces
7 interfaces between chains.
- C–D · 2235 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 2183 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 2108 Ų buried · 19 hydrogen bonds · protein-protein
- A–G · 2079 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 2011 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
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 P97372
- Elsewhere: RCSB PDB 5MSK · PDBe 5MSK · UniProt P97372
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