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Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+
Analyse Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GVS
- Type
- protein
- Length
- 4,406 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q21A49
- Ligands
- NAP, K
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F, H, I | — | protein | 441 | — | Q21A49 |
| B, D, G, J | — | protein | 440 | — | Q21A49 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- K · Potassium ion · metal · 10 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GVS · Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+ · the same entry in another collection · 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 Q21A49
- Elsewhere: RCSB PDB 6GVS · PDBe 6GVS · UniProt Q21A49
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