Structure of PDB 4gph Chain C

Receptor sequence
>4gphC (length=212) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
TATAGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLF
YTALEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITA
SPAVIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYG
VDPEALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFV
FNHQVFADLGKG
3D structure
PDB4gph Crystal Structures of the Substrate-Free and the Product-Bound forms of HmuO, a Heme Oxygenase from Corynebacterium diphtheriae
ChainC
Resolution1.7 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) H23 Y51 V129 R130 G133 D134 G138
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 BLA C K613 H620 Y730 L734 G735 S738 I743 R777 F801 N804 F808 K11 H18 Y128 L132 G133 S136 I141 R175 F199 N202 F206
BS02 ASC C H620 E624 H18 E22
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:4gph, PDBe:4gph, PDBj:4gph
PDBsum4gph
PubMed
UniProtQ54AI1

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