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A serpin structure

Analyse A serpin structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HGC
Type
protein
Length
373 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serpin
UniProt
H0ZQY2
Ligands
HCY, BDG, SO4
Pockets
3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerpinprotein37332% helix, 30% strandH0ZQY2

Ligands and binding sites

  • HCY · (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione · ligand · chains A
  • BDG · 2,6-diamino-2,6-dideoxy-alpha-D-glucopyranose · ligand · chains A
  • SO4 · Sulfate ion · ion · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11480.500.7817HCY
2580.290.7518SO4
3510.270.7413empty

Compared structures

  • 5HGC · A Serpin structure · the same entry in another collection · chain A against A, TM-score 1.00

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