Research workbench
Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with N-[(2S)-2-pyrrolidinylmethyl]- trifluoromethanesulfonamide bound
Analyse Crystal structure of human aminoadipate semialdehyde synthase, saccharopine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O1N
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UDR5
- Ligands
- 9H8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 442 | — | Q9UDR5 |
Ligands and binding sites
- 9H8 · 1,1,1-tris(fluoranyl)-~{N}-[[(2~{S})-pyrrolidin-2-yl]methyl]methanesulfonamide · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O1N · Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UDR5 · AlphaFold monomer V2.0 prediction for alpha-aminoadipic semialdehyde synthase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9UDR5
- Elsewhere: RCSB PDB 5O1N · PDBe 5O1N · UniProt Q9UDR5
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