Research workbench
Free-wilson and structural approaches to co-optimising human and rodent isoform potency for 11B-hydroxysteroid dehydrogenase type 1 11B-HSD1 inhibitors
Analyse Free-wilson and structural approaches to co-optimising human and rodent isoform… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BB5
- Type
- protein
- Length
- 1,043 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Corticosteroid 11-beta-dehydrogenase isozyme 1
- EC
- 1.1.1.146
- UniProt
- P28845
- Ligands
- NAP, HD2
- Pockets
- 12 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) | protein | 263 | 51% helix, 15% strand | P28845 |
| B | Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) | protein | 264 | 52% helix, 14% strand | P28845 |
| C | Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) | protein | 254 | 53% helix, 14% strand | P28845 |
| D | Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) | protein | 262 | 51% helix, 13% strand | P28845 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- HD2 · 4-cyclopentyl-N-[(1S,3R)-5-oxidanyl-2-adamantyl]-2-[[(3S)-oxolan-3-yl]amino]pyrimidine-5-carboxamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 850 | 0.86 | 0.89 | 77 | NAP, HD2 |
| 2 | 607 | 0.84 | 0.89 | 58 | NAP, HD2 |
| 3 | 616 | 0.84 | 0.89 | 61 | NAP, HD2 |
| 4 | 1150 | 0.82 | 0.83 | 97 | empty |
| 5 | 736 | 0.79 | 0.83 | 58 | NAP, HD2 |
Interfaces
6 interfaces between chains.
- A–B · 3002 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2607 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 357 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 303 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 42 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4BB5 · Free-Wilson and Structural Approaches to Co-optimising Human and Rodent Isoform Potency… · the same entry in another collection · chain D against D, TM-score 1.00
- P28845 · AlphaFold monomer V2.0 prediction for corticosteroid 11-beta- dehydrogenase isozyme 1… · a predicted model of the same protein · chain D 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
- Every structure of UniProt P28845
- Elsewhere: RCSB PDB 4BB5 · PDBe 4BB5 · UniProt P28845
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.