Structure of PDB 5loq Chain B Binding Site BS01

Receptor Information
>5loq Chain B (length=233) Species: 1639 (Listeria monocytogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITKNIGE
GEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPTYSYI
SVVELSYQNKGVRARLYPALPPKKHICFYPMSKKRDGADNWYMLPMEERQ
QLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWGVTLFSDDALEFKRIVTE
MRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI
Ligand information
Ligand IDFEC
InChIInChI=1S/C36H38N4O8.Fe/c1-17-21(5-9-33(41)42)29-14-27-19(3)22(6-10-34(43)44)30(39-27)15-28-20(4)24(8-12-36(47)48)32(40-28)16-31-23(7-11-35(45)46)18(2)26(38-31)13-25(17)37-29;/h13-16H,5-12H2,1-4H3,(H6,37,38,39,40,41,42,43,44,45,46,47,48);/q;+4/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyFEDZMOFKVKOYTI-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c2cc3[n+]4c(cc5c(c(c6n5[Fe]47n2c(c1CCC(=O)O)cc8[n+]7c(c6)C(=C8CCC(=O)O)C)CCC(=O)O)C)C(=C3C)CCC(=O)O
CACTVS 3.341Cc1c(CCC(O)=O)c2C=C3C(=C(C)C4=[N+]3[Fe]56N7C(=CC8=[N+]5C(=Cc1n26)C(=C8CCC(O)=O)C)C(=C(CCC(O)=O)C7=C4)C)CCC(O)=O
OpenEye OEToolkits 1.5.0Cc1c2cc3[n+]4c(cc5c(c(c6n5[Fe@]47n2c(c1CCC(=O)O)cc8[n+]7c(c6)C(=C8CCC(=O)O)C)CCC(=O)O)C)C(=C3C)CCC(=O)O
ACDLabs 10.04O=C(O)CCC1=C(C7=[N+]3C1=Cc5c(c(c6C=C8[N+]4=C(C=C2C(=C(C(N2[Fe]34n56)=C7)CCC(=O)O)C)C(=C8C)CCC(=O)O)C)CCC(=O)O)C
CACTVS 3.341Cc1c(CCC(O)=O)c2C=C3C(=C(C)C4=[N+]3[Fe@]56N7C(=CC8=[N+]5C(=Cc1n26)C(=C8CCC(O)=O)C)C(=C(CCC(O)=O)C7=C4)C)CCC(O)=O
FormulaC36 H36 Fe N4 O8
Name1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX;
FE-COPROPORPHYRIN III
ChEMBL
DrugBank
ZINC
PDB chain5loq Chain B Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5loq Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		R133 Y147 M149 H174 G178 Y181 V185 Q187 W200 V202 L204 M219 S225 F231
Binding residue
(residue number reindexed from 1)		R115 Y129 M131 H156 G160 Y163 V167 Q169 W182 V184 L186 M201 S207 F213
Annotation score3
Enzymatic activity
Enzyme Commision number 1.3.98.5: hydrogen peroxide-dependent heme synthase.
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006783 heme biosynthetic process
GO:0098869 cellular oxidant detoxification

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5loq, PDBe:5loq, PDBj:5loq
PDBsum5loq
PubMed27758026
UniProtQ8Y5F1|CHDC_LISMO Coproheme decarboxylase (Gene Name=chdC)

[Back to BioLiP]