Structure of PDB 1iw0 Chain C

Receptor sequence
>1iw0C (length=207) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
GLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTAL
EQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPAV
IDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDPE
ALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNHQ
VFADLGK
3D structure
PDB1iw0 The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae.
ChainC
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) H625 Y653 V731 R732 G735 D736 G740
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 C K613 H620 A623 E624 Y730 V731 G735 S738 F801 F808 K7 H14 A17 E18 Y124 V125 G129 S132 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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