MolNFT v2 · #157467 · protein
Dimeric isocitrate dehydrogenase from Xanthomonas campestris pv. campestris 8004
6M3S: “Dimeric isocitrate dehydrogenase from Xanthomonas campestris pv. campestris 8004”. X-ray diffraction at 2.3, 2 ligands (NAD, ICA). MolNFT v2 #157467 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6M3S
- Type
- protein
- Length
- 671 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Xanthomonas campestris
- UniProt
- A0A2S4JWD6
- Ligands
- NAD, ICA
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 333 | — | A0A2S4JWD6 |
| B | — | protein | 338 | — | A0A2S4JWD6 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- ICA · Isocitrate calcium complex · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6M3S · Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. campestris 8004 · 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 A0A2S4JWD6
- Elsewhere: RCSB PDB 6M3S · PDBe 6M3S · UniProt A0A2S4JWD6
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