Structure of PDB 3sn0 Chain A

Receptor sequence
>3sn0A (length=401) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
SLKVVSVDTLCCDAGWRNYHFVKLTTDEGIVGWSEFDEGFGSPGVTAVIE
QLGKRLVGASVMEHERFFAEAYCLTRPATGGVVSEGIGAIENALLDAKAK
TLNVPCYELLGGKLRDRVPVYWSHCPTWRINHPKFFGPPVTDLDGVKRTA
EEARERQFRAIKTNIFIHDDGPLHAWRPGFAVPFQPALNVDRKVLRNLRA
HLEALRDGAGPDVEILLDLNFNAKPEGYLKILRELADFDLFWVEIDSYSP
QGLAYVRNHSPHPISSCETLFGIREFKPFFDANAVDVAIVDTIWNGVWQS
MKIAAFADAHDINVAPHNFYGHLCTMINANFAAAVPNLRIMETDIDRLAW
EDELFTHAPEYQNGELIIPDRPGWGTDPVEEAILAHPPKVMGGLLQYKRS
E
3D structure
PDB3sn0 Crystal structure of putative L-alanine-DL-glutamate epimerase from Burkholderia xenovorans strain LB400 bound to magnesium and fumarate
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K161 N163 D217 N219 E243 C266 E267 I288 D290 H316 E341 D343
Catalytic site (residue number reindexed from 1) K162 N164 D218 N220 E244 C267 E268 I289 D291 H317 E342 D344
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 MG A D217 E243 E267 D218 E244 E268
BS02 FUM A H123 N163 R176 F179 N219 H124 N164 R177 F180 N220
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3sn0, PDBe:3sn0, PDBj:3sn0
PDBsum3sn0
PubMed
UniProtQ13PB7

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