Research workbench
FE(II)/(ALPHA)KETOGLUTARATE-dependent dioxygenase ASQJ_V72I mutant in complex with cyclopeptin (1B)
Analyse FE(II)/(ALPHA)KETOGLUTARATE-dependent dioxygenase ASQJ_V72I mutant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OA7
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5AR53
- Ligands
- AKG, 58K, NI
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 288 | — | Q5AR53 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- 58K · cyclopeptin · ligand · chains A
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OA7 · Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ_V72I mutant in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5AR53 · AlphaFold monomer V2.0 prediction for IRON/ALPHA-ketoglutarate- dependent dioxygenase… · a predicted model of the same protein · 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 Q5AR53
- Elsewhere: RCSB PDB 5OA7 · PDBe 5OA7 · UniProt Q5AR53
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