MolNFT v2 · #153818 · protein
Crystal structure of enoyl-CoA hydratase (ECH) from Ralstonia eutropha H16 in complex with NAD
6IUN: “Crystal structure of enoyl-CoA hydratase (ECH) from Ralstonia eutropha H16 in complex with NAD”. X-ray diffraction at 2.38, 1 ligand (NAD). MolNFT v2 #153818 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IUN
- Type
- protein
- Length
- 1,384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.38
- Source
- Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
- UniProt
- Q0KBG3
- Ligands
- NAD
Structure
x-ray diffraction · resolution 2.38 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | — | protein | 692 | — | Q0KBG3 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains B, A
- GOL · Glycerol · additive · 6 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IUN · Crystal structure of enoyl-CoA hydratase (ech) from ralstonia eutropha H16 in complex… · 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 Q0KBG3
- Elsewhere: RCSB PDB 6IUN · PDBe 6IUN · UniProt Q0KBG3
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