Research workbench
Complex of active mutant (S215->C) of glucose 6-phosphate dehydrogenase from L.MESENTEROIDES with coenzyme NAD
Analyse Complex of active mutant (S215->C) of glucose 6-phosphate dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H94
- Type
- protein
- Length
- 485 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose 6-phosphate 1-dehydrogenase
- EC
- 1.1.1.49
- UniProt
- P11411
- Ligands
- NAD
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose 6-phosphate 1-dehydrogenase (EC 1.1.1.49) | protein | 485 | 41% helix, 19% strand | P11411 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.63 | 0.79 | 51 | empty |
| 2 | 108 | 0.39 | 0.75 | 18 | empty |
| 3 | 79 | 0.35 | 0.76 | 16 | NAD |
| 4 | 52 | 0.26 | 0.74 | 13 | empty |
Compared structures
- 1H94 · Complex of active mutant (S215->C) of glucose 6-phosphate dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P11411 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate 1-dehydrogenase (P11411) · a predicted model of the same protein · chain A 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 P11411
- Elsewhere: RCSB PDB 1H94 · PDBe 1H94 · UniProt P11411
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