MolNFT v1 · #71643 · protein
Crystal structure of mycobacterium tuberculosis proteasome with propetide and an T1A mutation at beta-subunit
3MKA · Proteasome subunit alpha: “Crystal structure of mycobacterium tuberculosis proteasome with propetide and an T1A mutation at beta-subunit”. X-ray diffraction, 20 pockets (best druggability 0.84). MolNFT v1 #71643 on GenesisL1: 3D…
- PDB
- 3MKA
- Type
- protein
- Length
- 6,579 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit alpha; Proteasome subunit beta
- EC
- 3.4.25.1
- UniProt
- O33244, O33245
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 25 distinct chains · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome subunit alpha (EC 3.4.25.1) | protein | 222 | 41% helix, 26% strand | O33244 |
| B | Proteasome subunit alpha (EC 3.4.25.1) | protein | 220 | 42% helix, 25% strand | O33244 |
| C, P | Proteasome subunit beta (EC 3.4.25.1) | protein | 250 | 38% helix, 28% strand | O33245 |
| D | Proteasome subunit alpha (EC 3.4.25.1) | protein | 222 | 43% helix, 26% strand | O33244 |
| E | Proteasome subunit beta (EC 3.4.25.1) | protein | 248 | 40% helix, 27% strand | O33245 |
| F, U | Proteasome subunit alpha (EC 3.4.25.1) | protein | 221 | 43% helix, 26% strand | O33244 |
| G | Proteasome subunit beta (EC 3.4.25.1) | protein | 251 | 38% helix, 27% strand | O33245 |
| H | Proteasome subunit beta (EC 3.4.25.1) | protein | 249 | 38% helix, 28% strand | O33245 |
| I | Proteasome subunit alpha (EC 3.4.25.1) | protein | 217 | 42% helix, 26% strand | O33244 |
| J | Proteasome subunit beta (EC 3.4.25.1) | protein | 252 | 38% helix, 27% strand | O33245 |
| K | Proteasome subunit alpha (EC 3.4.25.1) | protein | 221 | 43% helix, 26% strand | O33244 |
| L | Proteasome subunit beta (EC 3.4.25.1) | protein | 251 | 38% helix, 27% strand | O33245 |
| M, Y | Proteasome subunit alpha (EC 3.4.25.1) | protein | 224 | 43% helix, 25% strand | O33244 |
| N | Proteasome subunit beta (EC 3.4.25.1) | protein | 252 | 39% helix, 27% strand | O33245 |
| O | Proteasome subunit alpha (EC 3.4.25.1) | protein | 218 | 41% helix, 25% strand | O33244 |
| Q | Proteasome subunit alpha (EC 3.4.25.1) | protein | 222 | 41% helix, 26% strand | O33244 |
| R | Proteasome subunit beta (EC 3.4.25.1) | protein | 246 | 39% helix, 28% strand | O33245 |
| S | Proteasome subunit alpha (EC 3.4.25.1) | protein | 219 | 44% helix, 26% strand | O33244 |
| T | Proteasome subunit beta (EC 3.4.25.1) | protein | 250 | 40% helix, 28% strand | O33245 |
| V | Proteasome subunit beta (EC 3.4.25.1) | protein | 249 | 39% helix, 28% strand | O33245 |
| W | Proteasome subunit alpha (EC 3.4.25.1) | protein | 221 | 40% helix, 26% strand | O33244 |
| X | Proteasome subunit beta (EC 3.4.25.1) | protein | 249 | 39% helix, 26% strand | O33245 |
| Z | Proteasome subunit beta (EC 3.4.25.1) | protein | 245 | 41% helix, 26% strand | O33245 |
| 2 | Proteasome subunit beta (EC 3.4.25.1) | protein | 246 | 41% helix, 28% strand | O33245 |
| 1 | Proteasome subunit alpha (EC 3.4.25.1) | protein | 219 | 41% helix, 26% strand | O33244 |
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 | 621 | 0.84 | 0.89 | 50 | empty |
| 2 | 620 | 0.84 | 0.89 | 49 | empty |
| 3 | 617 | 0.83 | 0.88 | 49 | empty |
| 4 | 692 | 0.83 | 0.87 | 56 | empty |
| 5 | 653 | 0.83 | 0.87 | 45 | empty |
Interfaces
89 interfaces between chains.
- A–B · 1228 Ų buried · 14 hydrogen bonds · protein-protein
- D–Q · 1187 Ų buried · 20 hydrogen bonds · protein-protein
- F–W · 1157 Ų buried · 18 hydrogen bonds · protein-protein
- U–1 · 1142 Ų buried · 14 hydrogen bonds · protein-protein
- K–M · 1137 Ų buried · 19 hydrogen bonds · protein-protein
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 O33244
- Every structure of UniProt O33245
- Elsewhere: RCSB PDB 3MKA · PDBe 3MKA · UniProt O33244 · UniProt O33245
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