Structure of PDB 1yi9 Chain A

Receptor sequence

>1yi9A (length=295) Species: 10116 (Rattus norvegicus)

CLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVID
FKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAP
PTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRV
PQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHL
GKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFT
GEEICNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIP

3D structure

• PDB: 1yi9 The catalytic copper of Peptidylglycine alpha-Hydroxylating Monooxygenase also plays a critical structural role.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H107 H108 Q170 H172 H242 H244 I314
• Catalytic site (residue number reindexed from 1): H61 H62 Q124 H126 H196 H198 I254
• Enzyme Commision number: 1.14.17.3: peptidylglycine monooxygenase.
  4.3.2.5: peptidylamidoglycolate lyase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CU	A	H108 H172	H62 H126
BS02	CU	A	H242 H244	H196 H198

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:1yi9, PDBe:1yi9, PDBj:1yi9
• PDBsum: 1yi9
• PubMed: 16100265
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)