Structure of PDB 1dje Chain A

Receptor sequence
>1djeA (length=383) Species: 562 (Escherichia coli) [Search protein sequence]
SWQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLG
LSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSR
ALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFA
HNDVTHLARLLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWL
MVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTV
ADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITR
FRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPP
TVPAGIARLRLTLTAAHEMQDIDRLLEVLHGNG
3D structure
PDB1dje Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies.
ChainA
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N47 H133 E175 S179 D204 H207 K236
Catalytic site (residue number reindexed from 1) N46 H132 E174 S178 D203 H206 K235
Enzyme Commision number 2.3.1.47: 8-amino-7-oxononanoate synthase.
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 PLP A G108 F109 H133 E175 S179 D204 A206 H207 T233 K236 G107 F108 H132 E174 S178 D203 A205 H206 T232 K235
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008710 8-amino-7-oxononanoate synthase activity
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0009058 biosynthetic process
GO:0009102 biotin biosynthetic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1dje, PDBe:1dje, PDBj:1dje
PDBsum1dje
PubMed10642176
UniProtP12998|BIOF_ECOLI 8-amino-7-oxononanoate synthase (Gene Name=bioF)

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