Structure of PDB 5uc9 Chain C Binding Site BS01
Receptor Information
>5uc9 Chain C (length=210) Species:
9606
(Homo sapiens) [
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ADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSA
LEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKA
AQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYN
MQIFNELDQA
Ligand information
Ligand ID
MYR
InChI
InChI=1S/C14H28O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14(15)16/h2-13H2,1H3,(H,15,16)
InChIKey
TUNFSRHWOTWDNC-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.385
CCCCCCCCCCCCCC(O)=O
OpenEye OEToolkits 1.7.6
CCCCCCCCCCCCCC(=O)O
ACDLabs 12.01
O=C(O)CCCCCCCCCCCCC
Formula
C14 H28 O2
Name
MYRISTIC ACID
ChEMBL
CHEMBL111077
DrugBank
DB08231
ZINC
ZINC000001530417
PDB chain
5uc9 Chain C Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
5uc9
Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.
Resolution
1.903 Å
Binding residue
(original residue number in PDB)
Y134 R156 N230 I233 F234
Binding residue
(residue number reindexed from 1)
Y104 R126 N200 I203 F204
Annotation score
1
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
PDBsum
5uc9
PubMed
28132836
UniProt
P30519
|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)
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