Structure of PDB 3moo Chain B Binding Site BS03

Receptor Information
>3moo Chain B (length=209) Species: 1717 (Corynebacterium diphtheriae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATAGLAVELKQSTAQAHEKAEHSTFMSDLLKGRLGVAEFTRLQEQAWLFY
TALEQAVDAVRASGFAESLLDPALNRAEVLARDLDKLNGSSEWRSRITAS
PAVIDYVNRLEEIRDNVDGPALVAHHYVRYLGDLSGGQVIARMMQRHYGV
DPEALGFYHFEGIAKLKVYKDEYREKLNNLELSDEQREHLLKEATDAFVF
NHQVFADLG
Ligand information
Ligand IDVEA
InChIInChI=1S/C33H32N4O5.Fe/c1-7-20-19(6)32-37-27(20)14-25-18(5)23(10-12-31(40)41)29(35-25)15-28-22(9-11-30(38)39)17(4)24(34-28)13-26-16(3)21(8-2)33(36-26)42-32;/h7-8,13-15H,1-2,9-12H2,3-6H3,(H3-,34,35,36,37,38,39,40,41);/q;+6/p-1/b24-13-,25-14-,26-13-,27-14-,28-15-,29-15-;
InChIKeyOCHHJFVQYXRHAA-HPQJSUICSA-M
SMILES
SoftwareSMILES
CACTVS 3.370Cc1c2C=C3C(=C(C)C4=[N@+]3[Fe@@++]56n2c(C=C7C(=C(C)C(=[N@@+]57)C=C8[N@]6C(=[O+]4)C(=C8C)C=C)CCC(O)=O)c1CCC(O)=O)C=C
ACDLabs 12.01O=C(O)CCC1=C(C2=[n+]4c1cc8c(c(c7C=C5C(=C(c6[o+]c3C(\C=C)=C(C(=C2)n3[Fe+2]4([n+]56)n78)C)C)\C=C)C)CCC(=O)O)C
OpenEye OEToolkits 1.7.2Cc1c2cc3[n+]4c([o+]c5c(c(c6n5[Fe+2]47n2c(c1CCC(=O)O)cc8[n+]7c(c6)C(=C8CCC(=O)O)C)C)C=C)C(=C3C=C)C
OpenEye OEToolkits 1.7.2Cc1c2cc3[n+]4c([o+]c5c(c(c6n5[Fe@+2]47n2c(c1CCC(=O)O)cc8[n+]7c(c6)C(=C8CCC(=O)O)C)C)C=C)C(=C3C=C)C
CACTVS 3.370Cc1c2C=C3C(=C(C)C4=[N+]3[Fe++]56n2c(C=C7C(=C(C)C(=[N+]57)C=C8[N]6C(=[O+]4)C(=C8C)C=C)CCC(O)=O)c1CCC(O)=O)C=C
FormulaC33 H31 Fe N4 O5
Name5-OXA-PROTOPORPHYRIN IX CONTAINING FE
ChEMBL
DrugBank
ZINC
PDB chain3moo Chain B Residue 912 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3moo Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: a combined X-ray crystallography and QM/MM study.
Resolution1.71 Å
Binding residue
(original residue number in PDB)		K13 H20 E24 Y130 V131 G135 S138 G139 K173 R177 F201 F208
Binding residue
(residue number reindexed from 1)		K10 H17 E21 Y127 V128 G132 S135 G136 K170 R174 F198 F205
Annotation score2
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).
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3moo, PDBe:3moo, PDBj:3moo
PDBsum3moo
PubMed20806922
UniProtQ54AI1

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