Structure of PDB 5loq Chain D

Receptor sequence

>5loqD (length=250) Species: 1639 (Listeria monocytogenes) [Search protein sequence]

NEAVKTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITK
NIGEGEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPT
YSYISVVELSNYLASHMAGGDDPYQNKGVRARLYPALPPKKHICFYPMSK
KRDGADNWYMLPMEERQQLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWG
VTLFSDDALEFKRIVTEMRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI

3D structure

PDB

5loq Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.

Chain

Resolution

1.69 Å

3D
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Enzymatic activity

Enzyme Commision number

1.3.98.5: hydrogen peroxide-dependent heme synthase.

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	FEC	D	S111 Y113 L114 Y147 M149 K151 I171 H174 G178 V185 Q186 Q187 W200 L204 I215 M219 S225 F231	S110 Y112 L113 Y146 M148 K150 I170 H173 G177 V184 Q185 Q186 W199 L203 I214 M218 S224 F230

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

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Molecular Function

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Biological Process

External links

PDB	RCSB:5loq, PDBe:5loq, PDBj:5loq
PDBsum	5loq
PubMed	27758026
UniProt	Q8Y5F1\|CHDC_LISMO Coproheme decarboxylase (Gene Name=chdC)

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