Structure of PDB 6kmm Chain B Binding Site BS02

Receptor Information
>6kmm Chain B (length=361) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEQIVPFYGKHQAGITTAHQTYVYFAALDVTAKEKSDIITLFRNWTSLTQ
MLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPSFFEKDGKD
RFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRN
LLNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTEDDSLMN
SIVWVQSGEPDWMTGGTYMAFRKIKMFLEIWDRSSLKDQEDTFGRRKSSG
APFGQKKETDPVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGY
MDAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCK
KGEYIAQRLLE
Ligand information
Ligand IDOXY
InChIInChI=1S/O2/c1-2
InChIKeyMYMOFIZGZYHOMD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341
OpenEye OEToolkits 1.5.0		O=O
FormulaO2
NameOXYGEN MOLECULE
ChEMBLCHEMBL1234886
DrugBankDB09140
ZINC
PDB chain6kmm Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6kmm Characterization of dye-decolorizing peroxidase from Bacillus subtilis.
Resolution1.93 Å
Binding residue
(original residue number in PDB)		D187 R286
Binding residue
(residue number reindexed from 1)		D186 R285
Annotation score1
Enzymatic activity
Enzyme Commision number 1.11.1.-
4.98.1.1: protoporphyrin ferrochelatase.
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:6kmm, PDBe:6kmm, PDBj:6kmm
PDBsum6kmm
PubMed32971035
UniProtP39597|EFEB_BACSU Deferrochelatase (Gene Name=efeB)

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