MolNFT v2 · #129865 · protein
R. palustris Rpa4515 with adipate
5OKU: “R. palustris Rpa4515 with adipate”. X-ray diffraction at 2.07, 2 ligands (0L1, SO4). MolNFT v2 #129865 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OKU
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.07
- Source
- Rhodopseudomonas palustris CGA009
- UniProt
- Q6N193
- Ligands
- 0L1, SO4
Structure
x-ray diffraction · resolution 2.07 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | Q6N193 |
Ligands and binding sites
- 0L1 · hexanedioic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OKU · R. palustris RPA4515 with adipate · 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 Q6N193
- Elsewhere: RCSB PDB 5OKU · PDBe 5OKU · UniProt Q6N193
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