Structure of PDB 4e3q Chain C

Receptor sequence
>4e3qC (length=451) Species: 676 (Vibrio fluvialis) [Search protein sequence]
NKPQSWEARAETYSLYGFTDMPSLHQRGTVVVTHGEGPYIVDVNGRRYLD
ANSGLWNMVAGFDHKGLIDAAKAQYERFPGYHAFFGRMSDQTVMLSEKLV
EVSPFDSGRVFYTNSGSEANDTMVKMLWFLHAAEGKPQKRKILTRWNAYH
GVTAVSASMTGKPYNSVFGLPLPGFVHLTCPHYWRYGEEGETEEQFVARL
ARELEETIQREGADTIAGFFAEPVMGAGGVIPPAKGYFQAILPILRKYDI
PVISDEVICGFGRTGNTWGCVTYDFTPDAIISSKNLTAGFFPMGAVILGP
ELSKRLETAIEAIEEFPHGFTASGHPVGCAIALKAIDVVMNEGLAENVRR
LAPRFEERLKHIAERPNIGEYRGIGFMWALEAVKDKASKTPFDGNLSVSE
RIANTCTDLGLICRPLGQSVVLCPPFILTEAQMDEMFDKLEKALDKVFAE
V
3D structure
PDB4e3q Redesigning and characterizing the substrate specificity and activity of Vibrio fluvialis aminotransferase for the synthesis of imagabalin.
ChainC
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F19 Y150 E223 D256 I259 K285 T322 V422
Catalytic site (residue number reindexed from 1) F18 Y149 E222 D255 I258 K284 T321 V421
Enzyme Commision number ?
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 PMP C S116 G117 S118 Y150 H151 E223 D256 V258 I259 K285 S115 G116 S117 Y149 H150 E222 D255 V257 I258 K284
BS02 PMP C F321 T322 F320 T321
Gene Ontology
Molecular Function
GO:0004015 adenosylmethionine-8-amino-7-oxononanoate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009102 biotin biosynthetic process
GO:0009448 gamma-aminobutyric acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4e3q, PDBe:4e3q, PDBj:4e3q
PDBsum4e3q
PubMed23012440
UniProtF2XBU9

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