Structure of PDB 4gpc Chain B

Receptor sequence
>4gpcB (length=211) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
TAGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFYT
ALEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITASP
AVIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGVD
PEALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVFN
HQVFADLGKGL
3D structure
PDB4gpc Crystal Structures of the Substrate-Free and the Product-Bound forms of HmuO, a Heme Oxygenase from Corynebacterium diphtheriae
ChainB
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) H325 Y353 V431 R432 G435 D436 G440
Catalytic site (residue number reindexed from 1) H21 Y49 V127 R128 G131 D132 G136
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 B K313 H320 A323 E324 L333 Y430 V431 G435 S438 I443 R477 F501 F508 K9 H16 A19 E20 L29 Y126 V127 G131 S134 I139 R173 F197 F204
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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