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Structure of the trypsin-binding domain of bowman-birk type protease inhibitor and its interaction with trypsin

Analyse Structure of the trypsin-binding domain of bowman-birk type protease inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TAB
Type
protein
Length
259 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trypsin; Bowman-birk type proteinase inhibitor
EC
3.4.21.4
UniProt
P00760, P01058
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ETrypsin (EC 3.4.21.4)protein2239% helix, 35% strandP00760
IBowman-birk type proteinase inhibitorprotein360% helix, 19% strandP01058

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11490.440.7627empty

Interfaces

1 interface between chains.

  • E–I · 711 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 1TAB · Structure of the trypsin-binding domain of bowman-birk type protease inhibitor and its… · the same entry in another collection · chain E against E, TM-score 1.00
  • P01058 · AlphaFold monomer V2.0 prediction for bowman-birk type proteinase inhibitor (P01058) · a predicted model of the same protein · chain I against A, TM-score 0.55

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