Structure of PDB 5loq Chain D Binding Site BS01

Receptor Information
>5loq Chain D (length=250) Species: 1639 (Listeria monocytogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NEAVKTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITK
NIGEGEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPT
YSYISVVELSNYLASHMAGGDDPYQNKGVRARLYPALPPKKHICFYPMSK
KRDGADNWYMLPMEERQQLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWG
VTLFSDDALEFKRIVTEMRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI
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 D Residue 302 [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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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)		S111 Y113 L114 Y147 M149 K151 I171 H174 G178 V185 Q186 Q187 W200 L204 I215 M219 S225 F231
Binding residue
(residue number reindexed from 1)		S110 Y112 L113 Y146 M148 K150 I170 H173 G177 V184 Q185 Q186 W199 L203 I214 M218 S224 F230
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
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Biological Process
External links
PDB RCSB:5loq, PDBe:5loq, PDBj:5loq
PDBsum5loq
PubMed27758026
UniProtQ8Y5F1|CHDC_LISMO Coproheme decarboxylase (Gene Name=chdC)

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