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Structure of dimethylformamidase, tetramer, Y440A mutant

Analyse Structure of dimethylformamidase, tetramer, Y440A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LVD
Type
protein
Length
3,464 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N,N-dimethylformamidase large subunit; N,N-dimethylformamidase small subunit
EC
3.5.1.56
UniProt
I6NT79, I6NWZ0
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 2 distinct chains · 18% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GN,N-dimethylformamidase large subunit (EC 3.5.1.56)protein74713% helix, 31% strandI6NT79
B, D, F, HN,N-dimethylformamidase small subunit (EC 3.5.1.56)protein11953% helix, 6% strandI6NWZ0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19920.850.8687empty
211460.830.8496empty
311650.830.8492empty
411780.820.8386empty
58070.810.8476empty

Interfaces

14 interfaces between chains.

  • A–C · 2685 Ų buried · 19 hydrogen bonds · protein-protein
  • E–G · 2682 Ų buried · 22 hydrogen bonds · protein-protein
  • E–F · 1495 Ų buried · 15 hydrogen bonds · protein-protein
  • C–D · 1469 Ų buried · 16 hydrogen bonds · protein-protein
  • G–H · 1455 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6LVD · Structure of Dimethylformamidase, tetramer, Y440A mutant · the same entry in another collection · chain A against A, TM-score 1.00

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