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Catalytic domain of human phosphodiesterase 1B
Analyse Catalytic domain of human phosphodiesterase 1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TAZ
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALCIUM/CALMODULIN-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- EC
- 3.1.4.17
- UniProt
- Q01064
- Ligands
- ZN, MG
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALCIUM/CALMODULIN-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (EC 3.1.4.17) | protein | 322 | 74% helix, 0% strand | Q01064 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.63 | 0.81 | 31 | MG |
| 2 | 63 | 0.38 | 0.79 | 17 | empty |
| 3 | 51 | 0.31 | 0.77 | 14 | empty |
| 4 | 53 | 0.28 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
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 Q01064
- Elsewhere: RCSB PDB 1TAZ · PDBe 1TAZ · UniProt Q01064
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