Structure of PDB 2dw7 Chain L

Receptor sequence
>2dw7L (length=388) Species: 375 (Bradyrhizobium japonicum) [Search protein sequence]
SVRIVDVREITKPISSPIRNAYIDFTKMTTSLVAVVTDVVREGKRVVGYG
FNSNGRYGQGGLIRERFASRILEADPKKLLNEAGDNLDPDKVWAAMMINE
KPGGHGERSVAVGTIDMAVWDAVAKIAGKPLFRLLAERHGVKANPRVFVY
AAGGYYYPGKGLSMLRGEMRGYLDRGYNVVKMKIGGAPIEEDRMRIEAVL
EEIGKDAQLAVDANGRFNLETGIAYAKMLRDYPLFWYEEVGDPLDYALQA
ALAEFYPGPMATGENLFSHQDARNLLRYGGMRPDRDWLQFDCALSYGLCE
YQRTLEVLKTHGWSPSRCIPHGGHQMSLNIAAGLGLGGNESYPDLFQPYG
GFPDGVRVENGHITMPDLPGIGFEGKSDLYKEMKALAE
3D structure
PDB2dw7 Evolution of Enzymatic Activities in the Enolase Superfamily: d-Tartrate Dehydratase from Bradyrhizobium japonicum
ChainL
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N55 K182 K184 D213 N215 E239 G264 E265 D292 H322 E341 D345
Catalytic site (residue number reindexed from 1) N54 K181 K183 D212 N214 E238 G263 E264 D291 H321 E340 D344
Enzyme Commision number 4.2.1.81: D(-)-tartrate dehydratase.
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 L D213 E239 E265 D212 E238 E264
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0047808 D(-)-tartrate dehydratase activity
Biological Process
GO:0051260 protein homooligomerization

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Molecular Function
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Biological Process
External links
PDB RCSB:2dw7, PDBe:2dw7, PDBj:2dw7
PDBsum2dw7
PubMed17144653
UniProtQ89FH0|TARD_BRADU D(-)-tartrate dehydratase (Gene Name=tarD)

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