Structure of PDB 8dsj Chain K Binding Site BS02

Receptor Information

>8dsj Chain K (length=306) Species: 10116 (Rattus norvegicus)

NECGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFK
PRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPT
RLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQ
PLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGK
VVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGE
GRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPA
EANIPI

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 8dsj Chain K Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 8dsj New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.
• Resolution: 2.8 Å
• Binding residue (original residue number in PDB): H242 H244 M314
• Binding residue (residue number reindexed from 1): H194 H196 M266
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 1.14.17.3: peptidylglycine monooxygenase.
  4.3.2.5: peptidylamidoglycolate lyase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004497 monooxygenase activity
• GO:0005507 copper ion binding
• GO:0016715 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen

Biological Process

• GO:0006518 peptide metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:8dsj, PDBe:8dsj, PDBj:8dsj
• PDBsum: 8dsj
• PubMed: 36880254
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)