Structure of PDB 1tzz Chain B Binding Site BS01
Receptor Information
>1tzz Chain B (length=379) Species:
375
(Bradyrhizobium japonicum) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
SVRIVDVREITKPISSTKMTTSLVAVVTDVVREGKRVVGYGFNSNGRYGQ
GGLIRERFASRILEADPKKLLNEAGDNLDPDKVWAAMMINEKPGGHGERS
VAVGTIDMAVWDAVAKIAGKPLFRLLAERHGVKANPRVFVYAAGGYYYPG
KGLSMLRGEMRGYLDRGYNVVKMKIGGAPIEEDRMRIEAVLEEIGKDAQL
AVDANGRFNLETGIAYAKMLRDYPLFWYEEVGDPLDYALQAALAEFYPGP
MATGENLFSHQDARNLLRYGGMRPDRDWLQFDCALSYGLCEYQRTLEVLK
THGWSPSRCIPHGGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVRVE
NGHITMPDLPGIGFEGKSDLYKEMKALAE
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1tzz Chain B Residue 3502 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1tzz
Crystal structure of the protein L1841, unknown member of enolase superfamily from Bradyrhizobium japonicum
Resolution
1.86 Å
Binding residue
(original residue number in PDB)
D2216 E2242 E2268
Binding residue
(residue number reindexed from 1)
D203 E229 E255
Annotation score
1
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.
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1tzz
,
PDBe:1tzz
,
PDBj:1tzz
PDBsum
1tzz
PubMed
UniProt
Q89FH0
|TARD_BRADU D(-)-tartrate dehydratase (Gene Name=tarD)
[
Back to BioLiP
]