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Cryo-EM structure of dfga-B at 2.54 ångström resolution

Analyse Cryo-EM structure of dfga-B at 2.54 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DRE
Type
protein
Length
1,572 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sugar phosphate ISOMERASE/EPIMERASE; Dfgb
UniProt
I5AX50, I5AX49
Pockets
14 · best druggability 0.85

Structure

electron microscopy · 2 distinct chains · 34% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GSugar phosphate ISOMERASE/EPIMERASEprotein27644% helix, 19% strandI5AX50
B, D, F, HDfgbprotein1179% helix, 53% strandI5AX49

Pockets

14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16460.850.9081empty
28070.850.8890empty
36580.720.7975empty
46030.720.8065empty
52710.670.8333empty

Interfaces

20 interfaces between chains.

  • A–D · 842 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 842 Ų buried · 5 hydrogen bonds · protein-protein
  • E–H · 829 Ų buried · 4 hydrogen bonds · protein-protein
  • F–G · 829 Ų buried · 5 hydrogen bonds · protein-protein
  • G–H · 780 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7DRE · Cryo-EM structure of DfgA-B at 2.54 angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00

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