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The crystal structure of dehydrogenase from sinorhizobium meliloti

Analyse The crystal structure of dehydrogenase from sinorhizobium meliloti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UOE
Type
protein
Length
658 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dehydrogenase
UniProt
Q930Q4
Pockets
4 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADehydrogenaseprotein33945% helix, 20% strandQ930Q4
BDehydrogenaseprotein31943% helix, 20% strandQ930Q4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11780.840.9728empty
24620.680.7953empty
33720.640.7937empty
41860.510.7741empty

Interfaces

1 interface between chains.

  • A–B · 3163 Ų buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

  • 3UOE · The crystal structure of dehydrogenase from Sinorhizobium meliloti · the same entry in another collection · chain A against A, TM-score 1.00

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