Structure of PDB 4gpf Chain C

Receptor sequence
>4gpfC (length=208) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
AGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYTA
LEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASPA
VIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVDP
EALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFNH
QVFADLGK
3D structure
PDB4gpf Crystal Structure of the Substrate-Free and the Product-Bound forms of HmuO, a Heme Oxygenase from Corynebacterium diphtheriae
ChainC
Resolution1.9 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) H20 Y48 V126 R127 G130 D131 G135
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 A623 E624 Y730 V731 L734 G735 S738 G739 I743 R777 F801 F808 K8 H15 A18 E19 Y125 V126 L129 G130 S133 G134 I138 R172 F196 F203
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:4gpf, PDBe:4gpf, PDBj:4gpf
PDBsum4gpf
PubMed
UniProtQ54AI1

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