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N, N-dimethylformamidase

Analyse N, N-dimethylformamidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LVV
Type
protein
Length
7,096 residues
Chains
16
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.8
Source
Paracoccus sp. SSG05
Molecule
N,N-dimethylformamidase large subunit; N,N-dimethylformamidase small subunit
EC
3.5.1.56
UniProt
I6NT79, I6NWZ0
Ligands
FE
Pockets
20 · best druggability 0.90

Structure

x-ray diffraction · resolution 2.8 · 2 distinct chains · 21% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, K, M, ON,N-dimethylformamidase large subunit (EC 3.5.1.56)protein76216% helix, 33% strandI6NT79
B, D, F, H, J, L, N, PN,N-dimethylformamidase small subunit (EC 3.5.1.56)protein12549% helix, 14% strandI6NWZ0

Ligands and binding sites

  • FE · Fe (III) ion · metal · 8 copies · chains A, C, E, G, I, K, M, O
  • EDO · 1,2-ethanediol · additive · 8 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17680.900.9492empty
28160.900.9399empty
37350.890.9388empty
47580.890.9389empty
58870.820.8485empty

Interfaces

31 interfaces between chains.

  • E–G · 2937 Ų buried · 25 hydrogen bonds · protein-protein
  • M–O · 2936 Ų buried · 24 hydrogen bonds · protein-protein
  • I–K · 2931 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 2914 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 2073 Ų buried · 35 hydrogen bonds · protein-protein

Compared structures

  • 6LVV · N, N-dimethylformamidase · the same entry in another collection · chain A against A, TM-score 1.00

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