Structure of PDB 2q32 Chain B Binding Site BS01

Receptor Information
>2q32 Chain B (length=218) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSA
LEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAPKA
AQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYN
MQIFNELDQAGSTLARET
Ligand information
Ligand IDOXN
InChIInChI=1S/C34H62O11/c1-33(2,3)30-34(4,5)31-6-8-32(9-7-31)45-29-28-44-27-26-43-25-24-42-23-22-41-21-20-40-19-18-39-17-16-38-15-14-37-13-12-36-11-10-35/h6-9,35H,10-30H2,1-5H3
InChIKeyIVKNZCBNXPYYKL-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O(c1ccc(cc1)C(C)(C)CC(C)(C)C)CCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
OpenEye OEToolkits 1.5.0CC(C)(C)CC(C)(C)c1ccc(cc1)OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
CACTVS 3.341CC(C)(C)CC(C)(C)c1ccc(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)cc1
FormulaC34 H62 O11
NameOXTOXYNOL-10;
ALPHA-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXYPOLY(OXY-1,2-ETHANEDIYL);
TRITON X-100
ChEMBLCHEMBL1235043
DrugBank
ZINCZINC000058633062
PDB chain2q32 Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2q32 Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		V54 L74 Y134 R156 G159 D160 G163 L167 A226 F227 N230 I233 F234
Binding residue
(residue number reindexed from 1)		V24 L44 Y104 R126 G129 D130 G133 L137 A196 F197 N200 I203 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2q32, PDBe:2q32, PDBj:2q32
PDBsum2q32
PubMed17965015
UniProtP30519|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)

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