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The refined 2.0 ångströms X-ray crystal structure of the complex formed between bovine beta-trypsin and cmti-I, a trypsin inhibitor from squash seeds (cucurbita maxima): topological similarity of the squash seed inhibitors with the carboxypeptidase a inhibitor from potatoes

Analyse The refined 2.0 ångströms X-ray crystal structure of the complex formed between… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PPE
Type
protein
Length
252 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trypsin; Trypsin inhibitor cmti-I
EC
3.4.21.4
UniProt
P00760, P01074
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ETrypsin (EC 3.4.21.4)protein22310% helix, 35% strandP00760
ITrypsin inhibitor cmti-Iprotein2910% helix, 21% strandP01074

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.350.7819empty

Interfaces

1 interface between chains.

  • E–I · 867 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 1PPE · The refined 2.0 ångströms X-ray crystal structure of the complex formed between bovine… · the same entry in another collection · chain E against E, TM-score 1.00
  • P01074 · AlphaFold monomer V2.0 prediction for trypsin inhibitor 1 (P01074) · a predicted model of the same protein · chain I against A, TM-score 0.92

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