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Crystal structure of H172A phm (cuh absent, cum present)

Analyse Crystal structure of H172A phm (cuh absent, cum present) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6AMP
Type
protein
Length
304 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, 4.3.2.5
UniProt
P14925
Ligands
CU
Pockets
2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-glycine alpha-amidating monooxygenase (EC 1.14.17.3, 4.3.2.5)protein3044% helix, 48% strandP14925

Ligands and binding sites

  • CU · Copper (II) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12070.520.7745empty
2560.270.7315empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 6AMP · Crystal structure of H172A PHM (CuH absent, CuM present) · 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 0.97

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