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Laminin A2LG45 C-form, G6/7 bound.

Analyse Laminin A2LG45 C-form, G6/7 bound. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IK5
Type
protein
Length
379 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laminin subunit alpha-2
UniProt
Q60675
Ligands
4MU, NAG, BDP, XYS, A2G, GAL, CA
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALaminin subunit alpha-2protein3792% helix, 50% strandQ60675

Ligands and binding sites

  • 4MU · 7-hydroxy-4-methyl-2H-chromen-2-one · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BDP · beta-D-glucopyranuronic acid · sugar · 2 copies · chains A
  • XYS · alpha-D-xylopyranose · sugar · 2 copies · chains A
  • A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
  • GAL · beta-D-galactopyranose · sugar
  • CA · Calcium ion · metal · 2 copies · chains A
  • GOL · Glycerol · additive · 6 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.530.8318empty
21820.470.7624empty

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation, O-glycosylation).

Compared structures

  • 5IK5 · Laminin A2LG45 C-form, G6/7 bound. · the same entry in another collection · chain A against A, TM-score 1.00

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