Structure of PDB 1xk1 Chain A

Receptor sequence
>1xk1A (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
PQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYV
ALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTP
AMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSHGQVLKKIAQKALDLPS
SGEGLAFFTFPNIASATKFKQLYESRMNSLEMTPAVRQRVIEEAKTAFLL
NIQLFEELQELLTH
3D structure
PDB1xk1 Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity.
ChainA
Resolution2.08 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 D140 G144
Catalytic site (residue number reindexed from 1) N21 Y49 T126 R127 G130 D131 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 M34 Q38 Y134 G139 H143 F207 N210 K9 H16 E20 M25 Q29 Y125 G130 H134 F198 N201
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:1xk1, PDBe:1xk1, PDBj:1xk1
PDBsum1xk1
PubMed15690204
UniProtP09601|HMOX1_HUMAN Heme oxygenase 1 (Gene Name=HMOX1)

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