Structure of PDB 3kd3 Chain B Binding Site BS01

Receptor Information
>3kd3 Chain B (length=216) Species: 119856 (Francisella tularensis subsp. tularensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKNIIFDFDSTLIKKESLELILEPILQKSPAKLKEIEYITNLGMQGDISF
RDSLQKRLAIASPTKQSIKEFSNKYCPNLLTDGIKELVQDLKNKGFEIWI
FSGGLSESIQPFADYLNIPRENIFAVETIWNSDGSFKELDNSNGACDSKL
SAFDKAKGLIDGEVIAIGDGYTDYQLYEKGYATKFIAYMEHIEREKVINL
SKYVARNVAELASLIM
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3kd3 Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3kd3 Crystal structure of a phosphoserine phosphohydrolase-like protein from Francisella tularensis subsp. tularensis SCHUS4
Resolution1.7 Å
Binding residue
(original residue number in PDB)
D7 D9 D169
Binding residue
(residue number reindexed from 1)
D7 D9 D169
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D7 F8 D9 G103 D173
Catalytic site (residue number reindexed from 1) D7 F8 D9 G103 D173
Enzyme Commision number 3.1.3.3: phosphoserine phosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006564 L-serine biosynthetic process
GO:0016311 dephosphorylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3kd3, PDBe:3kd3, PDBj:3kd3
PDBsum3kd3
PubMed
UniProtQ5NH99

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