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Studies on an artificial trypsin inhibitor peptide derived from the mung bean inhibitor

Analyse Studies on an artificial trypsin inhibitor peptide derived from the mung bean… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SMF
Type
protein
Length
232 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trypsin; Bowman-birk type trypsin inhibitor
EC
3.4.21.4
UniProt
P00760, P01062
Ligands
CA

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ETrypsin (EC 3.4.21.4)protein22311% helix, 36% strandP00760
IBowman-birk type trypsin inhibitorprotein90% helix, 11% strandP01062

Ligands and binding sites

  • CA · Calcium ion · metal · chains E

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

Interfaces

1 interface between chains.

  • E–I · 505 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

  • 1SMF · Studies on an artificial trypsin inhibitor peptide derived from the mung bean inhibitor · the same entry in another collection · chain E against E, TM-score 1.00
  • P01062 · AlphaFold monomer V2.0 prediction for bowman-birk type trypsin inhibitor (P01062) · a predicted model of the same protein · chain I against A, TM-score 0.82

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