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The X-ray Crystallographic Structure of Branching Enzyme

Analyse The X-ray Crystallographic Structure of Branching Enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1M7X
Type
protein
Length
2,341 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.3
Source
Escherichia coli
Molecule
1,4-alpha-glucan Branching Enzyme
EC
2.4.1.18
UniProt
P07762
Pockets
20 · best druggability 0.84

Structure

x-ray diffraction · resolution 2.3 · 4 distinct chains · 27% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A1,4-alpha-glucan Branching Enzyme (EC 2.4.1.18)protein58728% helix, 24% strandP07762
B1,4-alpha-glucan Branching Enzyme (EC 2.4.1.18)protein59127% helix, 25% strandP07762
C1,4-alpha-glucan Branching Enzyme (EC 2.4.1.18)protein57824% helix, 23% strandP07762
D1,4-alpha-glucan Branching Enzyme (EC 2.4.1.18)protein58528% helix, 24% strandP07762

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15940.840.9074empty
24210.810.8942empty
33280.780.8941empty
43200.780.8938empty
54000.730.8438empty

Interfaces

4 interfaces between chains.

  • A–B · 1117 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 1014 Ų buried · 14 hydrogen bonds · protein-protein
  • B–D · 548 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 167 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1M7X · The X-ray crystallographic structure of branching enzyme · the same entry in another collection · chain D against D, TM-score 1.00
  • P07762 · AlphaFold monomer V2.0 prediction for 1,4-alpha-glucan branching enzyme glgb (P07762) · a predicted model of the same protein · chain B against A, TM-score 0.99

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