Structure of PDB 2qpp Chain A

Receptor sequence
>2qppA (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
RMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTY
SALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAP
KAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLP
STGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFE
YNMQIFNELDQAGS
3D structure
PDB2qpp Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
ChainA
Resolution2.61 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) N22 Y50 T127 R128 G131 D132 G136
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 HEM A H45 E49 V54 Y154 T155 R156 G159 S162 K199 R203 F227 F234 H17 E21 V26 Y126 T127 R128 G131 S134 K171 R175 F199 F206
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:2qpp, PDBe:2qpp, PDBj:2qpp
PDBsum2qpp
PubMed17965015
UniProtP30519|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)

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