Structure of PDB 6ala Chain C

Receptor sequence

>6alaC (length=304) Species: 10116 (Rattus norvegicus)

PVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRAS
MDTVHAMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPK
GVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIA
GMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSG
YRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTE
ATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANI
PIPV

3D structure

• PDB: 6ala Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
• Chain: C
• Resolution: 2.59 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H107 A108 Q170 H172 H242 H244 M314
• Catalytic site (residue number reindexed from 1): H55 A56 Q118 H120 H190 H192 M262
• 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	C	H107 H242 H244	H55 H190 H192
BS02	FLC	C	Y79 A108 H172 R240 H242 H244 M314 Y318	Y27 A56 H120 R188 H190 H192 M262 Y266

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:6ala, PDBe:6ala, PDBj:6ala
• PDBsum: 6ala
• PubMed: 30271955
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)