Research workbench
N-terminal splice region of rat C-AMP phosphodiesterase, NMR, 7 structures
Analyse N-terminal splice region of rat C-AMP phosphodiesterase, NMR, 7 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LOI
- Type
- protein
- Length
- 25 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic 3',5'-AMP specific phosphodiesterase RD1
- EC
- 3.1.4.17
- UniProt
- P54748
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic 3',5'-AMP specific phosphodiesterase RD1 (EC 3.1.4.17) | protein | 25 | 60% helix, 0% strand | P54748 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1LOI · N-terminal splice region of rat C-AMP phosphodiesterase, NMR, 7 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P54748 · AlphaFold monomer V2.0 prediction for camp-specific 3',5'-cyclic phosphodiesterase 4A… · a predicted model of the same protein · chain A against A, TM-score 0.38
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 P54748
- Elsewhere: RCSB PDB 1LOI · PDBe 1LOI · UniProt P54748
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