Research workbench
Crystal structure of mycobacterial tuberculosis proteasome
Analyse Crystal structure of mycobacterial tuberculosis proteasome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FHG
- Type
- protein
- Length
- 6,188 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 20S proteasome, alpha and beta subunits; Proteasome, beta subunit
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, F, I, K, M, O, Q, S, U, W, Y, 1 | 20S proteasome, alpha and beta subunits | protein | 220 | 40% helix, 23% strand | — |
| H, C, E, G, J, L, N, P, R, T, V, X, Z, 2 | Proteasome, beta subunit | protein | 222 | 36% helix, 29% strand | — |
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 | 565 | 0.83 | 0.89 | 48 | empty |
| 2 | 544 | 0.83 | 0.89 | 46 | empty |
| 3 | 551 | 0.83 | 0.88 | 49 | empty |
| 4 | 541 | 0.82 | 0.88 | 46 | empty |
| 5 | 544 | 0.82 | 0.88 | 50 | empty |
Interfaces
70 interfaces between chains.
- F–W · 930 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 925 Ų buried · 17 hydrogen bonds · protein-protein
- K–M · 918 Ų buried · 16 hydrogen bonds · protein-protein
- B–I · 910 Ų buried · 16 hydrogen bonds · protein-protein
- Q–Y · 898 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2FHG · Crystal Structure of Mycobacterial Tuberculosis Proteasome · the same entry in another collection · chain A against A, 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
- Elsewhere: RCSB PDB 2FHG · PDBe 2FHG
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