Structure of PDB 1oyl Chain A

Receptor sequence
>1oylA (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
PQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYV
ALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTP
AMQRYVKRLHEVGRTEPELLVAHAYTRYLGALSGGQVLKKIAQKALDLPS
SGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLL
NIQLFEELQELLTH
3D structure
PDB1oyl Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications
ChainA
Resolution1.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N30 Y58 T135 R136 G139 A140 G144
Catalytic site (residue number reindexed from 1) N21 Y49 T126 R127 G130 A131 G135
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 K18 H25 E29 Q38 Y134 T135 G139 S142 R183 F207 N210 F214 K9 H16 E20 Q29 Y125 T126 G130 S133 R174 F198 N201 F205
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:1oyl, PDBe:1oyl, PDBj:1oyl
PDBsum1oyl
PubMed12842469
UniProtP09601|HMOX1_HUMAN Heme oxygenase 1 (Gene Name=HMOX1)

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