Structure of PDB 8dsl Chain A Binding Site BS02

Receptor Information
>8dsl Chain A (length=310) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPEAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPI
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 chain8dsl Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8dsl New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.
Resolution2.05 Å
Binding residue
(original residue number in PDB)
H107 H108 H172
Binding residue
(residue number reindexed from 1)
H63 H64 H128
Annotation score1
Enzymatic activity
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

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Biological Process

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Cellular Component
External links
PDB RCSB:8dsl, PDBe:8dsl, PDBj:8dsl
PDBsum8dsl
PubMed36880254
UniProtP14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)

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