Structure of PDB 7e5q Chain B

Receptor sequence
>7e5qB (length=352) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EEQIVPFYGKHQAGITTAHQTYVYFAALDVTAKEKSDIITLFRNWTSLTQ
MLTSGKQRNQYLPPQDTGESADLSPSNLTVTFGFGPSFFEKDGKDRFGLK
SKKPKHLAALPALDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCE
VRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTEDDSLMNSIVWVQSGEP
DWMTGGTYMAFRKIKMFLEIWDRSSLKDQEDTFGRRKSSGAPFGQKKETD
PVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYMDAGLLFISF
QKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCKKGEYIAQRLL
ES
3D structure
PDB7e5q Structural insights at acidic pH of dye-decolorizing peroxidase from Bacillus subtilis.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.-
4.98.1.1: protoporphyrin ferrochelatase.
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 HEM B N181 K186 D187 G188 T189 G190 I225 M227 F244 H273 A277 K278 R286 L306 F308 F319 M322 L326 L332 N170 K175 D176 G177 T178 G179 I214 M216 F233 H262 A266 K267 R275 L295 F297 F308 M311 L315 L321
BS02 OXY B D187 R286 D176 R275
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
GO:0004601 peroxidase activity
GO:0016829 lyase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0033212 iron import into cell
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7e5q, PDBe:7e5q, PDBj:7e5q
PDBsum7e5q
PubMed36345957
UniProtP39597|EFEB_BACSU Deferrochelatase (Gene Name=efeB)

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