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Crystal structure of human pancreatic secretory protein ZG16B

Analyse Crystal structure of human pancreatic secretory protein ZG16B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AQG
Type
protein
Length
271 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Zymogen granule protein 16 homolog B
UniProt
Q96DA0
Ligands
PO4
Pockets
1 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AZymogen granule protein 16 homolog Bprotein1330% helix, 57% strandQ96DA0
BZymogen granule protein 16 homolog Bprotein1380% helix, 54% strandQ96DA0

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.400.7822empty

Interfaces

1 interface between chains.

  • A–B · 353 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 3AQG · Crystal structure of human pancreatic secretory protein ZG16b · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96DA0 · AlphaFold monomer V2.0 prediction for zymogen granule protein 16 homolog B (Q96DA0) · a predicted model of the same protein · chain A against A, TM-score 0.99

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