Structure of PDB 2q32 Chain B

Receptor sequence
>2q32B (length=218) Species: 9606 (Homo sapiens) [Search protein sequence]
ADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSA
LEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAPKA
AQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYN
MQIFNELDQAGSTLARET
3D structure
PDB2q32 Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 OXN B V54 L74 Y134 R156 G159 D160 G163 L167 A226 F227 N230 I233 F234 V24 L44 Y104 R126 G129 D130 G133 L137 A196 F197 N200 I203 F204
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:2q32, PDBe:2q32, PDBj:2q32
PDBsum2q32
PubMed17965015
UniProtP30519|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)

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