Structure of PDB 3mib Chain A Binding Site BS03
Receptor Information
>3mib Chain A (length=308) Species:
10116
(Rattus norvegicus) [
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NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFNHKDCSGVSVHLTRV
PQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHL
GKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFT
GEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTI
PAEANIPI
Ligand information
Ligand ID
NO2
InChI
InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1
InChIKey
IOVCWXUNBOPUCH-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
[O-]N=O
OpenEye OEToolkits 1.5.0
N(=O)[O-]
Formula
N O2
Name
NITRITE ION
ChEMBL
DrugBank
DB12529
ZINC
PDB chain
3mib Chain A Residue 1 [
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Receptor-Ligand Complex Structure
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PDB
3mib
Differential Reactivity Between the Two Copper Sites of Peptidylglycine alpha-Hydroxylating Monooxygenase (PHM)
Resolution
2.35 Å
Binding residue
(original residue number in PDB)
H242 H244 G308 M314
Binding residue
(residue number reindexed from 1)
H196 H198 G262 M268
Annotation score
1
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 H196 H198 M268
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:3mib
,
PDBe:3mib
,
PDBj:3mib
PDBsum
3mib
PubMed
20958070
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
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