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A structural basis for substrate and stereo selectivity in octopine dehydrogenase (odh-NADH-L-arginine)

Analyse A structural basis for substrate and stereo selectivity in octopine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3C7C
Type
protein
Length
403 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Octopine dehydrogenase
EC
1.5.1.11
UniProt
Q9BHM6
Ligands
NAD, ARG
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BOctopine dehydrogenase (EC 1.5.1.11)protein40339% helix, 20% strandQ9BHM6

Ligands and binding sites

  • NAD · Nicotinamide-adenine-dinucleotide · ligand · chains B
  • ARG · Arginine · ligand · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16760.690.7761NAD, ARG
2770.360.7618empty
3630.320.7520empty
4520.310.7718empty

Compared structures

  • 3C7C · A structural basis for substrate and stereo selectivity in octopine dehydrogenase… · the same entry in another collection · chain B against B, TM-score 1.00
  • Q9BHM6 · AlphaFold monomer V2.0 prediction for octopine dehydrogenase (Q9BHM6) · a predicted model of the same protein · chain B against A, TM-score 0.96

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