Research workbench
Human 20S-PA200 proteasome complex
Analyse Human 20S-PA200 proteasome complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6REY
- Type
- protein
- Length
- 9,562 residues
- Chains
- 30
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit alpha type-6; Proteasome subunit alpha type-2; Proteasome subunit…
- EC
- 3.4.25.1
- UniProt
- P60900, P25787, P25789, O14818, P28066, P25786, P25788, P28072, Q99436, P49720, P49721, P28074, P20618, P28070, Q14997
- Ligands
- IHP, K0W
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 15 distinct chains · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, O | Proteasome subunit alpha type-6 (EC 3.4.25.1) | protein | 234 | 38% helix, 26% strand | P60900 |
| B, P | Proteasome subunit alpha type-2 (EC 3.4.25.1) | protein | 214 | 36% helix, 27% strand | P25787 |
| C, Q | Proteasome subunit alpha type-4 (EC 3.4.25.1) | protein | 207 | 31% helix, 29% strand | P25789 |
| D, R | Proteasome subunit alpha type-7 (EC 3.4.25.1) | protein | 210 | 35% helix, 27% strand | O14818 |
| E, S | Proteasome subunit alpha type-5 (EC 3.4.25.1) | protein | 227 | 32% helix, 26% strand | P28066 |
| F, T | Proteasome subunit alpha type-1 (EC 3.4.25.1) | protein | 236 | 32% helix, 22% strand | P25786 |
| G, U | Proteasome subunit alpha type-3 (EC 3.4.25.1) | protein | 242 | 32% helix, 25% strand | P25788 |
| H, V | Proteasome subunit beta type-6 (EC 3.4.25.1) | protein | 198 | 33% helix, 34% strand | P28072 |
| I, W | Proteasome subunit beta type-7 (EC 3.4.25.1) | protein | 221 | 28% helix, 34% strand | Q99436 |
| J, X | Proteasome subunit beta type-3 (EC 3.4.25.1) | protein | 204 | 32% helix, 31% strand | P49720 |
| K, Y | Proteasome subunit beta type-2 (EC 3.4.25.1) | protein | 196 | 32% helix, 31% strand | P49721 |
| L, Z | Proteasome subunit beta type-5 (EC 3.4.25.1) | protein | 200 | 34% helix, 33% strand | P28074 |
| M, a | Proteasome subunit beta type-1 (EC 3.4.25.1) | protein | 213 | 30% helix, 33% strand | P20618 |
| N, b | Proteasome subunit beta type-4 (EC 3.4.25.1) | protein | 206 | 33% helix, 30% strand | P28070 |
| c, d | Proteasome activator complex subunit 4 | protein | 1773 | 55% helix, 1% strand | Q14997 |
Ligands and binding sites
- IHP · Inositol hexakisphosphate · ligand · 2 copies · chains c, d
- K0W · [(1~{S},2~{R},3~{R},4~{S},5~{S},6~{R})-2-[oxidanyl(phosphonooxy)phosphoryl]oxy-3,4,5,6-tetraphosphonooxy-cyclohexyl] phosphono hydrogen phosphate · ligand · 2 copies · chains c, d
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 | 937 | 0.84 | 0.86 | 108 | empty |
| 2 | 1115 | 0.84 | 0.84 | 123 | empty |
| 3 | 847 | 0.83 | 0.85 | 97 | empty |
| 4 | 1177 | 0.82 | 0.83 | 117 | empty |
| 5 | 256 | 0.80 | 0.92 | 30 | empty |
Interfaces
84 interfaces between chains.
- S–d · 1604 Ų buried · 17 hydrogen bonds · protein-protein
- E–c · 1596 Ų buried · 17 hydrogen bonds · protein-protein
- F–G · 1419 Ų buried · 21 hydrogen bonds · protein-protein
- T–U · 1416 Ų buried · 21 hydrogen bonds · protein-protein
- I–J · 1392 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 6REY · Human 20S-PA200 Proteasome Complex · 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 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 Q14997
- Elsewhere: RCSB PDB 6REY · PDBe 6REY · 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 Q14997
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.