Research workbench
Proteasome-activating nucleotidase (pan) N-domain (57-134) from archaeoglobus fulgidus fused to GCN4, P61A mutant
Analyse Proteasome-activating nucleotidase (pan) N-domain (57-134) from archaeoglobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WG6
- Type
- protein
- Length
- 1,044 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control protein GCN4, proteasome-activating nucleotidase
- EC
- 3.6.4.8
- UniProt
- P03069, O28303
- Pockets
- 3 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | General control protein GCN4, proteasome-activating nucleotidase (EC 3.6.4.8) | protein | 87 | 32% helix, 33% strand | P03069, O28303 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.45 | 0.75 | 32 | empty |
| 2 | 151 | 0.41 | 0.74 | 28 | empty |
| 3 | 131 | 0.39 | 0.74 | 26 | empty |
Interfaces
18 interfaces between chains.
- K–L · 1546 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 1546 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1545 Ų buried · 24 hydrogen bonds · protein-protein
- E–F · 1544 Ų buried · 23 hydrogen bonds · protein-protein
- G–H · 1544 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 2WG6 · Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus… · the same entry in another collection · chain K against K, 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 P03069
- Every structure of UniProt O28303
- Elsewhere: RCSB PDB 2WG6 · PDBe 2WG6 · UniProt P03069 · UniProt O28303
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