Structure of PDB 6kmn Chain A

Receptor sequence
>6kmnA (length=361) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EQIVPFYGKHQAGITTAHQTYVYFAALDVTAKEKSDIITLFRNWTSLTQM
LTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPSFFEKDGKDR
FGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNL
LNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTEDDSLMNS
IVWVQSGEPDWMTGGTYMAFRKIKMFLEIWDRSSLKDQEDTFGRRKSSGA
PFGQKKETDPVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYM
DAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCKK
GEYIAQRLLES
3D structure
PDB6kmn Characterization of dye-decolorizing peroxidase from Bacillus subtilis.
ChainA
Resolution2.44 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 1.11.1.-
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 K186 G188 T189 G190 I225 M227 F244 H273 R286 L306 F308 M322 L326 L332 K184 G186 T187 G188 I223 M225 F242 H271 R284 L304 F306 M320 L324 L330
BS02 OXY A D187 R286 D185 R284
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6kmn, PDBe:6kmn, PDBj:6kmn
PDBsum6kmn
PubMed32971035
UniProtP39597|EFEB_BACSU Deferrochelatase (Gene Name=efeB)

[Back to BioLiP]