- PDB-1lnz: Structure of the Obg GTP-binding protein -
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Basic information
Entry
Database: PDB / ID: 1lnz
Title
Structure of the Obg GTP-binding protein
Components
SPO0B-associated GTP-binding protein
Keywords
CELL CYCLE / GTPase / Obg / stringent factor / stress response / sporulation / large G-protein / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC
Function / homology
Function and homology information
sporulation resulting in formation of a cellular spore / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / ribosome biogenesis / GTPase activity / GTP binding / magnesium ion binding / cytoplasm Similarity search - Function
: / GTP-binding protein OBG, C-terminal / GTP-binding protein OBG, C-terminal domain superfamily / Domain of unknown function (DUF1967) / Obg C-terminal (OCT) domain profile. / Spo0b-associated Gtp-binding Protein; Chain: A, / GTP1/OBG domain / GTP1/OBG, conserved site / GTP1/OBG family signature. / GTP1/OBG domain ...: / GTP-binding protein OBG, C-terminal / GTP-binding protein OBG, C-terminal domain superfamily / Domain of unknown function (DUF1967) / Obg C-terminal (OCT) domain profile. / Spo0b-associated Gtp-binding Protein; Chain: A, / GTP1/OBG domain / GTP1/OBG, conserved site / GTP1/OBG family signature. / GTP1/OBG domain / GTP-binding protein Obg/CgtA / GTP1/OBG domain superfamily / GTP1/OBG / Obg domain profile. / OBG-type guanine nucleotide-binding (G) domain / OBG-type guanine nucleotide-binding (G) domain profile. / 50S ribosome-binding GTPase / GTP binding domain / Distorted Sandwich / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homology
SPO0B-associatedGTP-bindingprotein / GTP-binding protein obg
Mass: 38109.434 Da / Num. of mol.: 2 / Fragment: residues 1- 342 of P20964 / Mutation: selenomethionine substituted Source method: isolated from a genetically manipulated source Details: Full-length protein, residues 1-428, was purified and prepartively proteolyzed with subtilisin to obtain the 1-342 fragment Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P20964
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