Research workbench
Catalytic domain of human phosphodiesterase 4B in complex with AMP
Analyse Catalytic domain of human phosphodiesterase 4B in complex with AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TB5
- Type
- protein
- Length
- 646 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-specific 3',5'-cyclic phosphodiesterase 4B
- EC
- 3.1.4.17
- UniProt
- Q07343
- Ligands
- AMP, ZN, MG
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Camp-specific 3',5'-cyclic phosphodiesterase 4B (EC 3.1.4.17) | protein | 323 | 68% helix, 1% strand | Q07343 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.69 | 0.82 | 36 | MG, AMP |
| 2 | 438 | 0.67 | 0.79 | 50 | MG, AMP |
| 3 | 314 | 0.61 | 0.78 | 46 | empty |
| 4 | 155 | 0.56 | 0.81 | 20 | empty |
| 5 | 60 | 0.33 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 856 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1TB5 · Catalytic Domain Of Human Phosphodiesterase 4B In Complex With AMP · the same entry in another collection · chain A against A, TM-score 1.00
- Q07343 · AlphaFold monomer V2.0 prediction for camp-specific 3',5'-cyclic phosphodiesterase 4B… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q07343
- Elsewhere: RCSB PDB 1TB5 · PDBe 1TB5 · UniProt Q07343
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