Structure of PDB 1wzg Chain A

Receptor sequence
>1wzgA (length=209) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
GLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTAL
EQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPAV
IDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDPE
ALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNHQ
VFADLGKGL
3D structure
PDB1wzg Design of metal cofactors activated by a protein-protein electron transfer system.
ChainA
Resolution1.75 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 YOM A H20 E24 V131 L134 G135 S138 G139 F201 N204 F208 H14 E18 V125 L128 G129 S132 G133 F195 N198 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:1wzg, PDBe:1wzg, PDBj:1wzg
PDBsum1wzg
PubMed16769893
UniProtP71119|HMUO_CORDI Heme oxygenase (Gene Name=hmuO)

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