Structure of PDB 1phm Chain A Binding Site BS03

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 IDAZI
InChIInChI=1S/N3/c1-3-2/q-1
InChIKeyIVRMZWNICZWHMI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[N-]=[N+]=[N-]
FormulaN3
NameAZIDE ION
ChEMBLCHEMBL79455
DrugBank
ZINC
PDB chain1phm Chain A Residue 361 [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]
PDB1phm Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		H235 D282
Binding residue
(residue number reindexed from 1)		H186 D233
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1phm, PDBe:1phm, PDBj:1phm
PDBsum1phm
PubMed9360928
UniProtP14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)

[Back to BioLiP]