MolNFT v1 · #140468 · protein
FE(II)/(ALPHA)KETOGLUTARATE-dependent dioxygenase prha-V150L/A232S in complex with preaustinoid A3
5YBR: “FE(II)/(ALPHA)KETOGLUTARATE-dependent dioxygenase prha-V150L/A232S in complex with preaustinoid A3”. X-ray diffraction, 3 ligands (AKG, 8T9, FE). MolNFT v1 #140468 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5YBR
- Type
- protein
- Length
- 582 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1E1FFL0
- Ligands
- AKG, 8T9, FE
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 295 | — | A0A1E1FFL0 |
| B | — | protein | 287 | — | A0A1E1FFL0 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · 2 copies · chains A, B
- 8T9 · preaustinoid A3 · ligand · 2 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YBR · Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with… · 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 A0A1E1FFL0
- Elsewhere: RCSB PDB 5YBR · PDBe 5YBR · UniProt A0A1E1FFL0
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