GL1X · GenesisL1 explorer

MolNFT v1 · #18763 · protein

Modulation of agrin function by alternative splicing and CA2+ binding

1PZ8: “Modulation of agrin function by alternative splicing and CA2+ binding”. X-ray diffraction, 1 ligand (CA), 6 pockets (best druggability 0.70). MolNFT v1 #18763 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
1PZ8
Type
protein
Length
708 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Agrin
UniProt
P31696
Ligands
CA
Pockets
6 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 3% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAgrinprotein1762% helix, 49% strandP31696
BAgrinprotein1792% helix, 47% strandP31696
CAgrinprotein1762% helix, 51% strandP31696
DAgrinprotein1775% helix, 50% strandP31696

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1810.700.9425empty
2850.570.8620empty
3830.500.8321empty
4600.440.8219empty
5540.330.7821empty

Interfaces

3 interfaces between chains.

  • B–D · 824 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 116 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 26 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1PZ8 · Modulation of agrin function by alternative splicing and Ca2+ binding · the same entry in another collection · chain D against D, TM-score 1.00
  • P31696 · AlphaFold monomer V2.0 prediction for agrin (P31696) · a predicted model of the same protein · chain A against A, TM-score 0.96

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