Structure of PDB 4gpc Chain A

Receptor sequence
>4gpcA (length=212) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
ATAGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFY
TALEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITAS
PAVIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGV
DPEALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVF
NHQVFADLGKGL
3D structure
PDB4gpc Crystal Structures of the Substrate-Free and the Product-Bound forms of HmuO, a Heme Oxygenase from Corynebacterium diphtheriae
ChainA
Resolution1.85 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) H22 Y50 V128 R129 G132 D133 G137
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 A K13 H20 E24 M29 L33 Y130 V131 G135 S138 G139 I143 R177 F201 F208 K10 H17 E21 M26 L30 Y127 V128 G132 S135 G136 I140 R174 F198 F205
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:4gpc, PDBe:4gpc, PDBj:4gpc
PDBsum4gpc
PubMed
UniProtQ54AI1

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