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Crystal and molecular structures of human progastricsin at 1.62 ångströms resolution

Analyse Crystal and molecular structures of human progastricsin at 1.62 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HTR
Type
protein
Length
372 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Progastricsin (pro segment); Gastricsin
EC
3.4.23.3
UniProt
P20142
Pockets
2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
PProgastricsin (pro segment) (EC 3.4.23.3)protein4340% helix, 16% strandP20142
BGastricsin (EC 3.4.23.3)protein32916% helix, 44% strandP20142

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15220.710.8056empty
2580.400.8115empty

Interfaces

1 interface between chains.

  • P–B · 2421 Ų buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1HTR · Crystal and molecular structures of human progastricsin at 1.62 ångströms resolution · the same entry in another collection · chain P against P, TM-score 1.00
  • P20142 · AlphaFold monomer V2.0 prediction for gastricsin (P20142) · a predicted model of the same protein · chain B against A, TM-score 0.95

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