Structure of PDB 1phm Chain A Binding Site BS02

Receptor Information
>1phm Chain A (length=305) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDINHKDCSGVSVHLTRVPQP
LIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKV
VSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEG
RTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAE
ANIPI
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 chain1phm Chain A Residue 358 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1phm Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		H242 H244 M314
Binding residue
(residue number reindexed from 1)		H193 H195 M265
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) H63 H64 Q126 H128 H193 H195 M265
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1phm, PDBe:1phm, PDBj:1phm
PDBsum1phm
PubMed9360928
UniProtP14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)

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