MolNFT v1 · #155099 · protein
Cryo-EM structure of human PA200
6KWX · Proteasome activator complex subunit 4: “Cryo-EM structure of human PA200”. Electron microscopy, 2 ligands (K0W, IHP), 20 pockets (best druggability 0.83). MolNFT v1 #155099 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6KWX
- Type
- protein
- Length
- 1,751 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome activator complex subunit 4
- UniProt
- Q14997
- Ligands
- K0W, IHP
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 57% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome activator complex subunit 4 | protein | 1751 | 57% helix, 1% strand | Q14997 |
Ligands and binding sites
- 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 · chains A
- IHP · Inositol hexakisphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 829 | 0.83 | 0.85 | 95 | empty |
| 2 | 991 | 0.75 | 0.77 | 97 | IHP |
| 3 | 951 | 0.72 | 0.76 | 83 | K0W |
| 4 | 215 | 0.70 | 0.86 | 30 | empty |
| 5 | 203 | 0.66 | 0.84 | 32 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 Q14997
- Elsewhere: RCSB PDB 6KWX · PDBe 6KWX · UniProt Q14997
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