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Structural basis for sugar translocation through maltoporin channels at 3.1 ångströms resolution

Analyse Structural basis for sugar translocation through maltoporin channels at 3.1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MAL
Type
protein
Length
1,263 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maltoporin
UniProt
P02943
Pockets
12 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 61% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CMaltoporinprotein4212% helix, 61% strandP02943

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11430.810.9820empty
26550.640.7483empty
35870.620.7470empty
45490.610.7464empty
52230.540.7729empty

Interfaces

3 interfaces between chains.

  • B–C · 1932 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 1929 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1928 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1MAL · Structural basis for sugar translocation through maltoporin channels at 3.1 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02943 · AlphaFold monomer V2.0 prediction for maltoporin (P02943) · a predicted model of the same protein · chain A against A, TM-score 1.00

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