MolNFT v1 · #133339 · protein
Pandda analysis group deposition -- crystal structure of DHTKD1 in complex with Z437516460
5RVY: “Pandda analysis group deposition -- crystal structure of DHTKD1 in complex with Z437516460”. X-ray diffraction, 3 ligands (TPP, NWY, MG). MolNFT v1 #133339 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5RVY
- Type
- protein
- Length
- 1,734 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96HY7
- Ligands
- TPP, NWY, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 867 | — | Q96HY7 |
| B | — | protein | 867 | — | Q96HY7 |
Ligands and binding sites
- TPP · Thiamine diphosphate · ligand · 2 copies · chains A, B
- NWY · N-[(6-methylpyridin-3-yl)methyl]cyclobutanecarboxamide · ligand · chains B
- MG · Magnesium ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5RVY · PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z437516460 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96HY7 · AlphaFold monomer V2.0 prediction for probable 2-oxoglutarate dehydrogenase E1 component… · a predicted model of the same protein · chain B 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 Q96HY7
- Elsewhere: RCSB PDB 5RVY · PDBe 5RVY · UniProt Q96HY7
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