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The three-dimensional structure of recombinant bovine chymosin at 2.3 ångströms resolution

Analyse The three-dimensional structure of recombinant bovine chymosin at 2.3 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CMS
Type
protein
Length
323 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Prochymosin A/B precursor
EC
3.4.23.4
UniProt
P00794
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProchymosin A/B precursor (EC 3.4.23.4)protein32315% helix, 48% strandP00794

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11310.400.7423empty
2850.340.7520empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1CMS · The three-dimensional structure of recombinant bovine chymosin at 2.3 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • P00794 · AlphaFold monomer V2.0 prediction for chymosin (P00794) · a predicted model of the same protein · chain A against A, TM-score 0.97

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