Structure of PDB 3i6d Chain B

Receptor sequence
>3i6dB (length=419) Species: 1423 (Bacillus subtilis) [Search protein sequence]
KKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVK
KDGYIIERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLH
PMPKGSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLS
GIYAGDIDKLSLMSTFPQFYQTQGQFQTLSTGLQTLVEEIEKQLKLTKVY
KGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAIS
HLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKK
WPHAAPEGKTLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEP
EMTCVTRWHESMPQYHVGHKQRIKELREALASAYPGVYMTGASFEGVGIP
DCIDQGKAAVSDALTYLFS
3D structure
PDB3i6d Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis
ChainB
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.3.15: coproporphyrinogen III oxidase (coproporphyrin-forming).
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 FAD B G12 G14 I15 T16 E41 A42 G48 K49 G63 P64 D65 S66 K255 V256 A285 P286 A289 W409 A443 V448 I450 C453 G8 G10 I11 T12 E37 A38 G44 K45 G59 P60 D61 S62 K204 V205 A234 P235 A238 W358 A392 V397 I399 C402
BS02 ACJ B K71 I176 M413 K67 I152 M362
Gene Ontology
Molecular Function
GO:0004729 oxygen-dependent protoporphyrinogen oxidase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0006783 heme biosynthetic process
Cellular Component
GO:0005737 cytoplasm
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:3i6d, PDBe:3i6d, PDBj:3i6d
PDBsum3i6d
PubMed19944166
UniProtP32397|CGOX_BACSU Coproporphyrinogen III oxidase (Gene Name=cgoX)

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