Structure of PDB 3mig Chain A Binding Site BS02

Receptor Information
>3mig Chain A (length=309) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVI
DFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNA
PPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTR
VPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVF
TGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRT
IPAEANIPI
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain3mig Chain A Residue 358 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3mig Differential Reactivity Between the Two Copper Sites of Peptidylglycine alpha-Hydroxylating Monooxygenase (PHM)
Resolution2.7 Å
Binding residue
(original residue number in PDB)		H242 H244
Binding residue
(residue number reindexed from 1)		H197 H199
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3mig, PDBe:3mig, PDBj:3mig
PDBsum3mig
PubMed20958070
UniProtP14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)

[Back to BioLiP]