Research workbench
Structure of USP14-bound human 26S proteasome in substrate-inhibited state SB_USP14
Analyse Structure of USP14-bound human 26S proteasome in substrate-inhibited state… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W3I
- Type
- protein
- Length
- 14,054 residues
- Chains
- 48
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.5
- Source
- Homo sapiens
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 14; 26S protease regulatory subunit 7; 26S protease…
- EC
- 3.4.19.12, 3.4.25.1, 3.4.19.-
- UniProt
- P54578, P35998, P62191, P62195, P43686, A0A087X2I1, P17980, P60900, P25787, P25789, O14818, P28066, P25786, P25788, P28072, Q99436, P49720, P49721, P28074, P20618, P28070, P0CG47, Q99460, O43242, O00232, O00231, Q15008, P51665, Q9UNM6, P55036, O00487, P48556, Q13200, P60896
- Ligands
- ATP, ADP, ZN
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · resolution 3.5 · 34 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| x | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) | protein | 494 | 26% helix, 23% strand | P54578 |
| A | 26S protease regulatory subunit 7 | protein | 413 | 36% helix, 11% strand | P35998 |
| B | 26S protease regulatory subunit 4 | protein | 399 | 37% helix, 13% strand | P62191 |
| C | Isoform 2 of 26S proteasome regulatory subunit 8 | protein | 386 | 39% helix, 13% strand | P62195 |
| D | 26S protease regulatory subunit 6B | protein | 380 | 39% helix, 15% strand | P43686 |
| E | 26S proteasome regulatory subunit 10B | protein | 389 | 44% helix, 14% strand | A0A087X2I1 |
| F | 26S protease regulatory subunit 6A | protein | 400 | 41% helix, 15% strand | P17980 |
| G, g | Proteasome subunit alpha type-6 (EC 3.4.25.1) | protein | 244 | 37% helix, 25% strand | P60900 |
| H, h | Proteasome subunit alpha type-2 (EC 3.4.25.1) | protein | 232 | 34% helix, 25% strand | P25787 |
| I, i | Proteasome subunit alpha type-4 (EC 3.4.25.1) | protein | 250 | 38% helix, 24% strand | P25789 |
| J, j | Proteasome subunit alpha type-7 (EC 3.4.25.1) | protein | 239 | 38% helix, 23% strand | O14818 |
| K, k | Proteasome subunit alpha type-5 (EC 3.4.25.1) | protein | 234 | 32% helix, 26% strand | P28066 |
| L, l | Isoform Long of Proteasome subunit alpha type-1 | protein | 238 | 33% helix, 24% strand | P25786 |
| M, m | Proteasome subunit alpha type-3 | protein | 240 | 35% helix, 26% strand | P25788 |
| N, n | Proteasome subunit beta type-6 (EC 3.4.25.1) | protein | 202 | 35% helix, 32% strand | P28072 |
| O, o | Proteasome subunit beta type-7 (EC 3.4.25.1) | protein | 220 | 29% helix, 33% strand | Q99436 |
| P, p | Proteasome subunit beta type-3 (EC 3.4.25.1) | protein | 204 | 30% helix, 28% strand | P49720 |
| Q, q | Proteasome subunit beta type-2 (EC 3.4.25.1) | protein | 199 | 32% helix, 33% strand | P49721 |
| R, r | Proteasome subunit beta type-5 (EC 3.4.25.1) | protein | 201 | 36% helix, 35% strand | P28074 |
| S, s | Proteasome subunit beta type-1 (EC 3.4.25.1) | protein | 213 | 30% helix, 30% strand | P20618 |
| T, t | Proteasome subunit beta type-4 (EC 3.4.25.1) | protein | 216 | 34% helix, 32% strand | P28070 |
| y | Ubiquitin | protein | 76 | 22% helix, 30% strand | P0CG47 |
| U | 26S proteasome non-ATPase regulatory subunit 1 | protein | 872 | 57% helix, 2% strand | Q99460 |
| V | 26S proteasome non-ATPase regulatory subunit 3 | protein | 444 | 71% helix, 2% strand | O43242 |
| W | 26S proteasome non-ATPase regulatory subunit 12 | protein | 446 | 64% helix, 2% strand | O00232 |
| X | 26S proteasome non-ATPase regulatory subunit 11 | protein | 380 | 72% helix, 3% strand | O00231 |
| Y | 26S proteasome non-ATPase regulatory subunit 6 | protein | 378 | 64% helix, 3% strand | Q15008 |
| Z | 26S proteasome non-ATPase regulatory subunit 7 | protein | 286 | 43% helix, 13% strand | P51665 |
| a | 26S proteasome non-ATPase regulatory subunit 13 | protein | 373 | 59% helix, 2% strand | Q9UNM6 |
| b | 26S proteasome non-ATPase regulatory subunit 4 | protein | 191 | 37% helix, 17% strand | P55036 |
| c | 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) | protein | 287 | 38% helix, 12% strand | O00487 |
| d | 26S proteasome non-ATPase regulatory subunit 8 | protein | 257 | 53% helix, 1% strand | P48556 |
| f | 26S proteasome non-ATPase regulatory subunit 2 | protein | 889 | 45% helix, 2% strand | Q13200 |
| e | 26S proteasome complex subunit DSS1 | protein | 50 | 20% helix, 0% strand | P60896 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, D, E, F
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B, C
- ZN · Zinc ion · metal · chains c
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 934 | 0.86 | 0.87 | 118 | empty |
| 2 | 1019 | 0.85 | 0.86 | 112 | empty |
| 3 | 1192 | 0.83 | 0.84 | 114 | ATP |
| 4 | 819 | 0.82 | 0.85 | 116 | empty |
| 5 | 871 | 0.82 | 0.84 | 88 | empty |
Interfaces
169 interfaces between chains.
- E–F · 4815 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 4354 Ų buried · 39 hydrogen bonds · protein-protein
- Z–c · 3604 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 2995 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 2764 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- P28070 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-4 (P28070) · a predicted model of the same protein · chain T against A, TM-score 0.99
- P20618 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-1 (P20618) · a predicted model of the same protein · chain S against A, TM-score 0.99
- P28072 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-6 (P28072) · a predicted model of the same protein · chain N against A, TM-score 0.99
- P25786 · AlphaFold monomer V2.0 prediction for proteasome subunit alpha type-1 (P25786) · a predicted model of the same protein · chain L against A, TM-score 0.99
- P49720 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-3 (P49720) · a predicted model of the same protein · chain P against A, TM-score 0.99
- P49721 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-2 (P49721) · a predicted model of the same protein · chain Q against A, TM-score 0.99
- P28074 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-5 (P28074) · a predicted model of the same protein · chain R against A, TM-score 0.99
- P25788 · AlphaFold monomer V2.0 prediction for proteasome subunit alpha type-3 (P25788) · a predicted model of the same protein · chain M against A, TM-score 0.98
- Q99436 · AlphaFold monomer V2.0 prediction for proteasome subunit beta type-7 (Q99436) · a predicted model of the same protein · chain O against A, TM-score 0.98
- P28066 · AlphaFold monomer V2.0 prediction for proteasome subunit alpha type-5 (P28066) · a predicted model of the same protein · chain K against A, TM-score 0.96
- O43242 · AlphaFold monomer V2.0 prediction for 26S proteasome non-ATPase regulatory subunit 3… · a predicted model of the same protein · chain V against A, TM-score 0.96
- P25787 · AlphaFold monomer V2.0 prediction for proteasome subunit alpha type-2 (P25787) · a predicted model of the same protein · chain H against A, TM-score 0.95
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 P54578
- Every structure of UniProt P35998
- Every structure of UniProt P62191
- Every structure of UniProt P62195
- Every structure of UniProt P43686
- Every structure of UniProt A0A087X2I1
- Every structure of UniProt P17980
- Every structure of UniProt P60900
- Every structure of UniProt P25787
- Every structure of UniProt P25789
- Every structure of UniProt O14818
- Every structure of UniProt P28066
- Every structure of UniProt P25786
- Every structure of UniProt P25788
- Every structure of UniProt P28072
- Every structure of UniProt Q99436
- Every structure of UniProt P49720
- Every structure of UniProt P49721
- Every structure of UniProt P28074
- Every structure of UniProt P20618
- Every structure of UniProt P28070
- Every structure of UniProt P0CG47
- Every structure of UniProt Q99460
- Every structure of UniProt O43242
- Every structure of UniProt O00232
- Every structure of UniProt O00231
- Every structure of UniProt Q15008
- Every structure of UniProt P51665
- Every structure of UniProt Q9UNM6
- Every structure of UniProt P55036
- Every structure of UniProt O00487
- Every structure of UniProt P48556
- Every structure of UniProt Q13200
- Every structure of UniProt P60896
- Elsewhere: RCSB PDB 7W3I · PDBe 7W3I · UniProt P54578 · UniProt P35998 · UniProt P62191 · UniProt P62195 · UniProt P43686 · UniProt A0A087X2I1 · UniProt P17980 · UniProt P60900 · UniProt P25787 · UniProt P25789 · UniProt O14818 · UniProt P28066 · UniProt P25786 · UniProt P25788 · UniProt P28072 · UniProt Q99436 · UniProt P49720 · UniProt P49721 · UniProt P28074 · UniProt P20618 · UniProt P28070 · UniProt P0CG47 · UniProt Q99460 · UniProt O43242 · UniProt O00232 · UniProt O00231 · UniProt Q15008 · UniProt P51665 · UniProt Q9UNM6 · UniProt P55036 · UniProt O00487 · UniProt P48556 · UniProt Q13200 · UniProt P60896
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