Research workbench
Glyceraldehyde-3-phosphate dehydrogenase mutant with cys 149 replaced by ala complexed with NAD+ and D-glyceraldehyde-3-phosphate
Analyse Glyceraldehyde-3-phosphate dehydrogenase mutant with cys 149 replaced by ala… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NQA
- 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, G3H
- Pockets
- 16 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 28% 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, 28% strand | P00362 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains O, R, P, Q
- G3H · Glyceraldehyde-3-phosphate · ligand · 4 copies · chains O, P, Q, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.74 | 0.81 | 54 | NAD, G3H |
| 2 | 79 | 0.74 | 0.97 | 20 | empty |
| 3 | 551 | 0.73 | 0.81 | 51 | NAD, G3H |
| 4 | 717 | 0.72 | 0.79 | 65 | NAD, G3H |
| 5 | 611 | 0.70 | 0.79 | 51 | NAD, G3H |
Interfaces
6 interfaces between chains.
- Q–R · 2152 Ų buried · 40 hydrogen bonds · protein-protein
- O–P · 2108 Ų buried · 36 hydrogen bonds · protein-protein
- P–Q · 1479 Ų buried · 21 hydrogen bonds · protein-protein
- O–R · 1474 Ų buried · 25 hydrogen bonds · protein-protein
- P–R · 539 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1NQA · Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ala Complexed… · 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 0.99
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 1NQA · PDBe 1NQA · UniProt P00362
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