Structure of PDB 6fxq Chain B

Receptor sequence
>6fxqB (length=233) Species: 169963 (Listeria monocytogenes EGD-e) [Search protein sequence]
KTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITKNIGE
GEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPTYSYI
SVVELSYQNKGVRARLYPALPPKKHICFYPMSKKRDGADNWYMLPMEERQ
QLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWGVTLFSDDALEFKRIVTE
MRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI
3D structure
PDB6fxq Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Hemeb.
ChainB
Resolution1.69 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B Y147 M149 H174 G178 Q187 W200 V202 M219 S225 F231 Y129 M131 H156 G160 Q169 W182 V184 M201 S207 F213
BS02 VOV B L110 S111 R133 Y147 M149 H174 G178 Q187 W200 V202 L204 M219 S225 F231 L105 S106 R115 Y129 M131 H156 G160 Q169 W182 V184 L186 M201 S207 F213
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:6fxq, PDBe:6fxq, PDBj:6fxq
PDBsum6fxq
PubMed31423350
UniProtQ8Y5F1|CHDC_LISMO Coproheme decarboxylase (Gene Name=chdC)

[Back to BioLiP]