- PDB-6g4j: Structure of the protein kinase YabT from Bacillus subtilis in co... -
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Basic information
Entry
Database: PDB / ID: 6g4j
Title
Structure of the protein kinase YabT from Bacillus subtilis in complex with an alphaREP crystallization helper
Components
Probable serine/threonine-protein kinase YabT
alphaREP bE8
Keywords
TRANSFERASE / Bacterial Hanks-type protein kinase / complex with an artificial binder / SIGNALING PROTEIN
Function / homology
Function and homology information
protein serine/threonine kinase activity => GO:0004674 / non-specific serine/threonine protein kinase / protein serine kinase activity / ATP binding Similarity search - Function
Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily Similarity search - Domain/homology
Evidence: gel filtration, The bE8 alphaREP binder makes tight and specific contacts with YabT
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Buried area
1710 Å2
ΔGint
-7 kcal/mol
Surface area
18040 Å2
Method
PISA
Unit cell
Length a, b, c (Å)
67.690, 122.870, 50.570
Angle α, β, γ (deg.)
90.000, 90.000, 90.000
Int Tables number
18
Space group name H-M
P21212
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Components
#1: Protein
Probableserine/threonine-proteinkinaseYabT
Mass: 35023.293 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The C-terminal transmembrane helix of YabT (residues 316-338) has been deleted. The juxtamembrane region (residues 274-315) is disordered. Source: (gene. exp.) Bacillus subtilis (strain 168) (bacteria) Strain: 168 / Gene: yabT, BSU00660 / Production host: Escherichia coli BL21(DE3) / Variant (production host): Rosetta References: UniProt: P37562, non-specific serine/threonine protein kinase
#2: Protein
alphaREPbE8
Mass: 15864.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The N-terminal His-tag and the C-terminal linker are disordered. Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
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