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Crystal structure analysis of the oxidized form of the M314I mutant of peptidylglycine alpha-hydroxylating monooxygenase

Analyse Crystal structure analysis of the oxidized form of the M314I mutant of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YI9
Type
protein
Length
295 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-glycine alpha-amidating monooxygenase
EC
1.14.17.3
UniProt
P14925
Ligands
CU
Pockets
4 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-glycine alpha-amidating monooxygenase (EC 1.14.17.3)protein2955% helix, 51% strandP14925

Ligands and binding sites

  • CU · Copper (II) ion · metal · 4 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.460.8519empty
21620.450.7529empty
3640.370.7815empty
4510.270.7415empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 1YI9 · Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine… · the same entry in another collection · chain A against A, TM-score 1.00
  • P14925 · AlphaFold monomer V2.0 prediction for peptidylglycine alpha-amidating monooxygenase… · a predicted model of the same protein · chain A against A, TM-score 0.96

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