Structure of PDB 1tzz Chain B

Receptor sequence
>1tzzB (length=379) Species: 375 (Bradyrhizobium japonicum) [Search protein sequence]
SVRIVDVREITKPISSTKMTTSLVAVVTDVVREGKRVVGYGFNSNGRYGQ
GGLIRERFASRILEADPKKLLNEAGDNLDPDKVWAAMMINEKPGGHGERS
VAVGTIDMAVWDAVAKIAGKPLFRLLAERHGVKANPRVFVYAAGGYYYPG
KGLSMLRGEMRGYLDRGYNVVKMKIGGAPIEEDRMRIEAVLEEIGKDAQL
AVDANGRFNLETGIAYAKMLRDYPLFWYEEVGDPLDYALQAALAEFYPGP
MATGENLFSHQDARNLLRYGGMRPDRDWLQFDCALSYGLCEYQRTLEVLK
THGWSPSRCIPHGGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVRVE
NGHITMPDLPGIGFEGKSDLYKEMKALAE
3D structure
PDB1tzz Crystal structure of the protein L1841, unknown member of enolase superfamily from Bradyrhizobium japonicum
ChainB
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) N2058 K2185 K2187 D2216 N2218 E2242 G2267 E2268 D2295 H2325 E2344 D2348
Catalytic site (residue number reindexed from 1) N45 K172 K174 D203 N205 E229 G254 E255 D282 H312 E331 D335
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 B D2216 E2242 E2268 D203 E229 E255
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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