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Anionic trypsin mutant with ser 214 replaced by lys

Analyse Anionic trypsin mutant with ser 214 replaced by lys in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ANC
Type
protein
Length
223 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P00763

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein223—P00763

Compared structures

  • 1ANC · Anionic trypsin mutant with ser 214 replaced by lys · the same entry in another collection · chain A against A, TM-score 1.00
  • P00763 · AlphaFold monomer V2.0 prediction for anionic trypsin-2 (P00763) · a predicted model of the same protein · chain A against A, TM-score 1.00

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