Structure of PDB 2xfo Chain B Binding Site BS03

Receptor Information
>2xfo Chain B (length=494) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVK
YVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGP
FPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELL
DKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIASTT
NGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNH
EMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYK
EPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKL
ARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYF
PPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILH
AMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLI
Ligand information
Ligand IDXCG
InChIInChI=1S/C11H8N2O/c1-2-4-9-8(3-1)7-10(14-9)11-12-5-6-13-11/h1-7H,(H,12,13)
InChIKeyVBFQIUOSXHUWCT-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04n1ccnc1c3oc2ccccc2c3
OpenEye OEToolkits 1.6.1c1ccc2c(c1)cc(o2)c3[nH]ccn3
CACTVS 3.352[nH]1ccnc1c2oc3ccccc3c2
FormulaC11 H8 N2 O
Name2-(2-BENZOFURANYL)-2-IMIDAZOLINE
ChEMBLCHEMBL151697
DrugBank
ZINCZINC000000017887
PDB chain2xfo Chain B Residue 1499 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2xfo Potentiation of ligand binding through cooperative effects in monoamine oxidase B.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L88 P102 F103 L164 L167 F168 A199 I316 Y326
Binding residue
(residue number reindexed from 1)		L86 P100 F101 L162 L165 F166 A197 I314 Y324
Annotation score1
Binding affinityMOAD: Ki=58uM
Enzymatic activity
Catalytic site (original residue number in PDB) G62 R197 K296
Catalytic site (residue number reindexed from 1) G60 R195 K294
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
1.4.3.4: monoamine oxidase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008131 primary methylamine oxidase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0050660 flavin adenine dinucleotide binding
GO:0052595 aliphatic amine oxidase activity
GO:0097621 monoamine oxidase activity
Biological Process
GO:0009410 response to xenobiotic stimulus
GO:0009636 response to toxic substance
GO:0010044 response to aluminum ion
GO:0010269 response to selenium ion
GO:0014063 negative regulation of serotonin secretion
GO:0019607 phenylethylamine catabolic process
GO:0021762 substantia nigra development
GO:0032496 response to lipopolysaccharide
GO:0042420 dopamine catabolic process
GO:0045471 response to ethanol
GO:0045964 positive regulation of dopamine metabolic process
GO:0048545 response to steroid hormone
GO:0050665 hydrogen peroxide biosynthetic process
GO:0051412 response to corticosterone
Cellular Component
GO:0005739 mitochondrion
GO:0005740 mitochondrial envelope
GO:0005741 mitochondrial outer membrane
GO:0030425 dendrite
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xfo, PDBe:2xfo, PDBj:2xfo
PDBsum2xfo
PubMed20855894
UniProtP27338|AOFB_HUMAN Amine oxidase [flavin-containing] B (Gene Name=MAOB)

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