MolNFT v1 · #55209 · protein
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, soaked with 2',3'-cyclic NADP
2YDB · 2', 3'-cyclic nucleotide 3'-phosphodiesterase: “Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, soaked with 2',3'-cyclic NADP”. X-ray diffraction, 1 ligand (NAP), 1 pocket (best druggability 0.55). MolNFT v1…
- PDB
- 2YDB
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2', 3'-cyclic nucleotide 3'-phosphodiesterase
- EC
- 3.1.4.37
- UniProt
- P16330
- Ligands
- NAP
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2', 3'-cyclic nucleotide 3'-phosphodiesterase (EC 3.1.4.37) | protein | 213 | 30% helix, 31% strand | P16330 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.55 | 0.78 | 41 | NAP |
Compared structures
- 2YDB · Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, soaked with… · the same entry in another collection · chain A against A, TM-score 1.00
- P16330 · AlphaFold monomer V2.0 prediction for 2',3'-cyclic-nucleotide 3'-phosphodiesterase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P16330
- Elsewhere: RCSB PDB 2YDB · PDBe 2YDB · UniProt P16330
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