Structure of PDB 1tzz Chain A

Receptor sequence
>1tzzA (length=374) Species: 375 (Bradyrhizobium japonicum) [Search protein sequence]
VRIVDVREITKPISSTKMTTSLVAVVTDVVREGKRVVGYGFNSNGRYGQG
GLIRERFASRILEADPKKLLNEAGDNLDPDKVWAAMMINEKPGGHGERSV
AVGTIDMAVWDAVAKIAGKPLFRLLAERHGVKANPRVFVYAAGGYYGLSM
LRGEMRGYLDRGYNVVKMKIGGAPIEEDRMRIEAVLEEIGKDAQLAVDAN
GRFNLETGIAYAKMLRDYPLFWYEEVGDPLDYALQAALAEFYPGPMATGE
NLFSHQDARNLLRYGGMRPDRDWLQFDCALSYGLCEYQRTLEVLKTHGWS
PSRCIPHGGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVRVENGHIT
MPDLPGIGFEGKSDLYKEMKALAE
3D structure
PDB1tzz Crystal structure of the protein L1841, unknown member of enolase superfamily from Bradyrhizobium japonicum
ChainA
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N1058 K1185 K1187 D1216 N1218 E1242 G1267 E1268 D1295 H1325 E1344 D1348
Catalytic site (residue number reindexed from 1) N44 K167 K169 D198 N200 E224 G249 E250 D277 H307 E326 D330
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 A D1216 E1242 E1268 D198 E224 E250
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:1tzz, PDBe:1tzz, PDBj:1tzz
PDBsum1tzz
PubMed
UniProtQ89FH0|TARD_BRADU D(-)-tartrate dehydratase (Gene Name=tarD)

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