Structure of PDB 1phm Chain A

Receptor sequence

>1phmA (length=305) Species: 10116 (Rattus norvegicus)

NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDINHKDCSGVSVHLTRVPQP
LIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKV
VSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEG
RTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAE
ANIPI

3D structure

• PDB: 1phm Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H107 H108 Q170 H172 H242 H244 M314
• Catalytic site (residue number reindexed from 1): H63 H64 Q126 H128 H193 H195 M265
• 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	H107 H108 H172	H63 H64 H128
BS02	CU	A	H242 H244 M314	H193 H195 M265
BS03	AZI	A	H235 D282	H186 D233

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:1phm, PDBe:1phm, PDBj:1phm
• PDBsum: 1phm
• PubMed: 9360928
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)