Research workbench
Crystal structure of the complex FE(II)/ALPHA-ketoglutarate dependent dioxygenase KDO1 with FE(II)/ALPHA-ketoglutarate
Analyse Crystal structure of the complex FE(II)/ALPHA-ketoglutarate dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F2B
- Type
- protein
- Length
- 1,279 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C7QJ42
- Ligands
- AKG, FE2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 325 | — | C7QJ42 |
| B | — | protein | 316 | — | C7QJ42 |
| C | — | protein | 326 | — | C7QJ42 |
| D | — | protein | 312 | — | C7QJ42 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · 4 copies · chains A, B, C, D
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6F2B · Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1… · the same entry in another collection · chain D against D, TM-score 1.00
- C7QJ42 · AlphaFold monomer V2.0 prediction for L-lysine 3-hydroxylase (C7QJ42) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 C7QJ42
- Elsewhere: RCSB PDB 6F2B · PDBe 6F2B · UniProt C7QJ42
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.