Structure of PDB 3i8r Chain A

Receptor sequence
>3i8rA (length=207) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
GLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTAL
EQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPAV
IDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDPE
ALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNHQ
VFADLGK
3D structure
PDB3i8r Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H25 Y53 V131 R132 G135 D136 G140
Catalytic site (residue number reindexed from 1) H19 Y47 V125 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 HEM A K13 H20 A23 L33 Y130 V131 G135 R177 F201 F208 K7 H14 A17 L27 Y124 V125 G129 R171 F195 F202
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006788 heme oxidation
GO:0006979 response to oxidative stress
GO:0042167 heme catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3i8r, PDBe:3i8r, PDBj:3i8r
PDBsum3i8r
PubMed20380462
UniProtQ54AI1

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