Structure of PDB 3moo Chain B

Receptor sequence
>3mooB (length=209) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence]
ATAGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFY
TALEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITAS
PAVIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGV
DPEALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVF
NHQVFADLG
3D structure
PDB3moo Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: a combined X-ray crystallography and QM/MM study.
ChainB
Resolution1.71 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 FRU B K13 A17 H20 E21 K10 A14 H17 E18
BS02 AZI B G135 G139 G132 G136
BS03 VEA B K13 H20 E24 Y130 V131 G135 S138 G139 K173 R177 F201 F208 K10 H17 E21 Y127 V128 G132 S135 G136 K170 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:3moo, PDBe:3moo, PDBj:3moo
PDBsum3moo
PubMed20806922
UniProtQ54AI1

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