Structure of PDB 6kmm Chain A

Receptor sequence
>6kmmA (length=361) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EQIVPFYGKHQAGITTAHQTYVYFAALDVTAKEKSDIITLFRNWTSLTQM
LTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPSFFEKDGKDR
FGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNL
LNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTEDDSLMNS
IVWVQSGEPDWMTGGTYMAFRKIKMFLEIWDRSSLKDQEDTFGRRKSSGA
PFGQKKETDPVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYM
DAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCKK
GEYIAQRLLES
3D structure
PDB6kmm Characterization of dye-decolorizing peroxidase from Bacillus subtilis.
ChainA
Resolution1.93 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 A N181 K186 G188 T189 G190 I225 F244 H273 A277 K278 R286 L306 F308 M322 L326 L332 N179 K184 G186 T187 G188 I223 F242 H271 A275 K276 R284 L304 F306 M320 L324 L330
BS02 EPE A T189 T260 K278 T187 T258 K276
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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