MolNFT v1 · #49546 · protein
Crystal structure of sulfate-bound saccharopine dehydrogenase (L-lys forming) from saccharomyces cerevisiae
2QRJ · Saccharopine dehydrogenase, NAD+, L-lysine-forming: “Crystal structure of sulfate-bound saccharopine dehydrogenase (L-lys forming) from saccharomyces cerevisiae”. X-ray diffraction, 2 ligands (SO4, CL), 1 pocket (best druggability…
- PDB
- 2QRJ
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Saccharopine dehydrogenase, NAD+, L-lysine-forming
- EC
- 1.5.1.7
- UniProt
- P38998
- Ligands
- SO4, CL
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Saccharopine dehydrogenase, NAD+, L-lysine-forming (EC 1.5.1.7) | protein | 365 | 36% helix, 14% strand | P38998 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.70 | 0.78 | 60 | SO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2QRJ · Crystal Structure of Sulfate-bound Saccharopine Dehydrogenase (L-Lys Forming) from… · the same entry in another collection · chain A against A, TM-score 1.00
- P38998 · AlphaFold monomer V2.0 prediction for saccharopine dehydrogenase [NAD(+)… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P38998
- Elsewhere: RCSB PDB 2QRJ · PDBe 2QRJ · UniProt P38998
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