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Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction
Analyse Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V4M
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C4NCJ7
- Ligands
- AKG, FE, K, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 168 | — | C4NCJ7 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains B
- FE · Fe (III) ion · metal · 2 copies · chains B
- K · Potassium ion · metal · chains B
- PO4 · Phosphate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7V4M · Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover… · the same entry in another collection · chain B against B, 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 C4NCJ7
- Elsewhere: RCSB PDB 7V4M · PDBe 7V4M · UniProt C4NCJ7
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