Structure of PDB 1iw0 Chain B

Receptor sequence
>1iw0B (length=209) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
GLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTAL
EQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPAV
IDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDPE
ALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNHQ
VFADLGKGL
3D structure
PDB1iw0 The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae.
ChainB
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H325 Y353 V431 R432 G435 D436 G440
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 GLC B K313 A317 H320 E321 K7 A11 H14 E15
BS02 HEM B K313 H320 E324 L333 Y430 V431 G435 G439 R477 F501 F508 K7 H14 E18 L27 Y124 V125 G129 G133 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:1iw0, PDBe:1iw0, PDBj:1iw0
PDBsum1iw0
PubMed14645223
UniProtP71119|HMUO_CORDI Heme oxygenase (Gene Name=hmuO)

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