Structure of PDB 3mig Chain A

Receptor sequence

>3migA (length=309) Species: 10116 (Rattus norvegicus)

ECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVI
DFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNA
PPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTR
VPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVF
TGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRT
IPAEANIPI

3D structure

• PDB: 3mig Differential Reactivity Between the Two Copper Sites of Peptidylglycine alpha-Hydroxylating Monooxygenase (PHM)
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H107 H108 Q170 H172 H242 H244 M314
• Catalytic site (residue number reindexed from 1): H62 H63 Q125 H127 H197 H199 M269
• 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	H62 H63 H127
BS02	CU	A	H242 H244	H197 H199
BS03	NO2	A	H242 H244 G308 M314	H197 H199 G263 M269
BS04	NO2	A	H235 D282	H190 D237

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:3mig, PDBe:3mig, PDBj:3mig
• PDBsum: 3mig
• PubMed: 20958070
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)