Research workbench
Glyceraldehyde-3-phosphate dehydrogenase mutant with asp 32 replaced by gly, leu 187 replaced by ala, and pro 188 replaced by ser complexed with NAD+
Analyse Glyceraldehyde-3-phosphate dehydrogenase mutant with asp 32 replaced by gly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DBV
- Type
- protein
- Length
- 1,336 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glyceraldehyde-3-phosphate dehydrogenase
- EC
- 1.2.1.12
- UniProt
- P00362
- Ligands
- NAD, SO4
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O, P, Q, R | Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) | protein | 334 | 30% helix, 30% strand | P00362 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains O, P, Q, R
- SO4 · Sulfate ion · ion · 8 copies · chains O, P, Q, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.76 | 0.97 | 28 | empty |
| 2 | 697 | 0.70 | 0.78 | 68 | SO4, NAD |
| 3 | 544 | 0.70 | 0.80 | 57 | SO4, NAD |
| 4 | 657 | 0.69 | 0.77 | 53 | SO4, NAD |
| 5 | 490 | 0.68 | 0.79 | 58 | SO4, NAD |
Interfaces
6 interfaces between chains.
- Q–R · 2123 Ų buried · 34 hydrogen bonds · protein-protein
- O–P · 2112 Ų buried · 35 hydrogen bonds · protein-protein
- O–R · 1433 Ų buried · 14 hydrogen bonds · protein-protein
- P–Q · 1409 Ų buried · 17 hydrogen bonds · protein-protein
- O–Q · 597 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1DBV · Glyceraldehyde-3-phosphate dehydrogenase mutant with asp 32 replaced by gly, leu 187… · the same entry in another collection · chain R against R, TM-score 1.00
- P00362 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P00362) · a predicted model of the same protein · chain O 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 P00362
- Elsewhere: RCSB PDB 1DBV · PDBe 1DBV · UniProt P00362
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.