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Trypsin at pH 5, 0.85 a

Analyse Trypsin at pH 5, 0.85 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PQ5
Type
protein
Length
224 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trypsin
EC
3.4.21.4
UniProt
P35049
Ligands
ARG, SO4

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATrypsin (EC 3.4.21.4)protein22410% helix, 37% strandP35049

Ligands and binding sites

  • ARG · Arginine · ligand · chains A
  • SO4 · Sulfate ion · ion · 3 copies · chains A

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

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1PQ5 · Trypsin at pH 5, 0.85 A · the same entry in another collection · chain A against A, TM-score 1.00
  • P35049 · AlphaFold monomer V2.0 prediction for trypsin (P35049) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

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