Research workbench
Binary complex of human glycerol 3-phosphate dehydrogenase, R269A mutant
Analyse Binary complex of human glycerol 3-phosphate dehydrogenase, R269A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PYP
- Type
- protein
- Length
- 685 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P21695
- Ligands
- NAD, 3SY, POP, K, PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 348 | — | P21695 |
| B | — | protein | 337 | — | P21695 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- 3SY · 2,2-bis(hydroxymethyl)propane-1,3-diol · ligand · chains A
- POP · Pyrophosphate 2- · ligand · chains B
- K · Potassium ion · metal · chains B
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PYP · Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P21695 · AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(+)]… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P21695
- Elsewhere: RCSB PDB 6PYP · PDBe 6PYP · UniProt P21695
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