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Trypsin specificity as elucidated by lie calculations, X-ray structures and association constant measurements

Analyse Trypsin specificity as elucidated by lie calculations, X-ray structures and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UTL
Type
protein
Length
222 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trypsin I
EC
3.4.21.4
UniProt
P35031
Ligands
PRA, CA
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
MTrypsin I (EC 3.4.21.4)protein2229% helix, 36% strandP35031

Ligands and binding sites

  • PRA · 3-phenylpropylamine · ligand · chains M
  • CA · Calcium ion · metal · chains M
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains M

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
1530.350.7817MPD

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1UTL · Trypsin specificity as elucidated by LIE calculations, X-ray structures and association… · the same entry in another collection · chain M against M, TM-score 1.00
  • P35031 · AlphaFold monomer V2.0 prediction for trypsin-1 (P35031) · a predicted model of the same protein · chain M against A, TM-score 0.99

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