Structure of PDB 5uc9 Chain A Binding Site BS01

Receptor Information
>5uc9 Chain A (length=209) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSA
LEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKA
AQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYN
MQIFNELDQ
Ligand information
Ligand IDMYR
InChIInChI=1S/C14H28O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14(15)16/h2-13H2,1H3,(H,15,16)
InChIKeyTUNFSRHWOTWDNC-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CCCCCCCCCCCCCC(O)=O
OpenEye OEToolkits 1.7.6CCCCCCCCCCCCCC(=O)O
ACDLabs 12.01O=C(O)CCCCCCCCCCCCC
FormulaC14 H28 O2
NameMYRISTIC ACID
ChEMBLCHEMBL111077
DrugBankDB08231
ZINCZINC000001530417
PDB chain5uc9 Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5uc9 Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.
Resolution1.903 Å
Binding residue
(original residue number in PDB)		L74 Y134 R156 L167 N230 F234
Binding residue
(residue number reindexed from 1)		L44 Y104 R126 L137 N200 F204
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N50 Y78 T155 R156 G159 D160 G164
Catalytic site (residue number reindexed from 1) N20 Y48 T125 R126 G129 D130 G134
Enzyme Commision number 1.14.14.18: heme oxygenase (biliverdin-producing).
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
Biological Process
GO:0006788 heme oxidation

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Molecular Function
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Biological Process
External links
PDB RCSB:5uc9, PDBe:5uc9, PDBj:5uc9
PDBsum5uc9
PubMed28132836
UniProtP30519|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)

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