Structure of PDB 1opm Chain A

Receptor sequence

>1opmA (length=310) Species: 10116 (Rattus norvegicus)

NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPI

3D structure

• PDB: 1opm Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase.
• Chain: A
• Resolution: 2.1 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 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	A	H107 H108 H172	H63 H64 H128
BS02	AZI	A	H235 D282	H191 D238
BS03	CU	A	H242 H244 M314	H198 H200 M270
BS04	IYG	A	F112 A135 L206 M208 R240 H242 M314 N316 Y318	F68 A91 L162 M164 R196 H198 M270 N272 Y274
BS05	IYG	A	L57 A63 K98 S190 V191 H192	L13 A19 K54 S146 V147 H148

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:1opm, PDBe:1opm, PDBj:1opm
• PDBsum: 1opm
• PubMed: 10504734
• UniProt: P14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)