Structure of PDB 5wja Chain D

Receptor sequence

>5wjaD (length=311) Species: 10116 (Rattus norvegicus)

NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVAHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPIP

3D structure

• PDB: 5wja Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
• Chain: D
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A107 H108 Q170 H172 H242 H244 M314
• Catalytic site (residue number reindexed from 1): A63 H64 Q126 H128 H198 H200 M270
• 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	D	H242 H244 M314	H198 H200 M270
BS02	FLC	D	Y79 H108 Q170 H172 R240 H242 Y318	Y35 H64 Q126 H128 R196 H198 Y274

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:5wja, PDBe:5wja, PDBj:5wja
• PDBsum: 5wja
• PubMed: 30271955
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)