MolNFT v1 · #24525 · protein
Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax
1UXV · Glyceraldehyde-3-phosphate dehydrogenase (NADP+): “Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating…”. X-ray diffraction, 3 ligands (NAP, AMP, NA), 2 pockets (best druggability 0.71).…
- PDB
- 1UXV
- Type
- protein
- Length
- 499 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glyceraldehyde-3-phosphate dehydrogenase (NADP+)
- EC
- 1.2.1.9
- UniProt
- O57693
- Ligands
- NAP, AMP, NA
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (EC 1.2.1.9) | protein | 499 | 39% helix, 23% strand | O57693 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.71 | 0.78 | 72 | NAP |
| 2 | 114 | 0.41 | 0.76 | 20 | AMP |
Compared structures
- 1UXV · Structural basis for allosteric regulation and substrate specificity of the… · the same entry in another collection · chain A against A, TM-score 1.00
- O57693 · AlphaFold monomer V2.0 prediction for NAD(P)-dependent glyceraldehyde-3-phosphate… · a predicted model of the same protein · chain A 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 O57693
- Elsewhere: RCSB PDB 1UXV · PDBe 1UXV · UniProt O57693
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