MolNFT v2 · #116903 · protein
Structure of the PLP-Dependent L-Arginine Hydroxylase MppP Holoenzyme
5DJ1: “Structure of the PLP-Dependent L-Arginine Hydroxylase MppP Holoenzyme”. X-ray diffraction at 2.102, 2 ligands (MG, CL). MolNFT v2 #116903 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5DJ1
- Type
- protein
- Length
- 1,421 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.102
- Source
- Streptomyces wadayamensis
- Ligands
- MG, CL
Structure
x-ray diffraction · resolution 2.102 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 351 | — | — |
| B, C | — | protein | 353 | — | — |
| D | — | protein | 364 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5DJ1 · Structure of the plp-dependent L-arginine hydroxylase mppp holoenzyme · 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
- Elsewhere: RCSB PDB 5DJ1 · PDBe 5DJ1
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