- PDB-1gku: Reverse gyrase from Archaeoglobus fulgidus -
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IDまたはキーワード:
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基本情報
登録情報
データベース: PDB / ID: 1gku
タイトル
Reverse gyrase from Archaeoglobus fulgidus
要素
REVERSE GYRASE
キーワード
TOPOISOMERASE / DNA SUPERCOILING / ARCHAEA / HELICASE
機能・相同性
機能・相同性情報
Isomerases; Isomerases altering macromolecular conformation; Enzymes altering nucleic acid conformation / reverse gyrase activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA unwinding involved in DNA replication / DNA topological change / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / cytoplasm 類似検索 - 分子機能
reverse gyrase domain / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 - #120 / EV matrix protein fold - #20 / EV matrix protein fold / Reverse gyrase / Reverse gyrase, TOPRIM domain / Zinc finger reverse gyrase N-terminal-type profile. / Zinc finger reverse gyrase C-terminal-type profile. / Topoisomerase I; domain 2 / Topoisomerase I, domain 2 ...reverse gyrase domain / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 - #120 / EV matrix protein fold - #20 / EV matrix protein fold / Reverse gyrase / Reverse gyrase, TOPRIM domain / Zinc finger reverse gyrase N-terminal-type profile. / Zinc finger reverse gyrase C-terminal-type profile. / Topoisomerase I; domain 2 / Topoisomerase I, domain 2 / Rossmann fold - #140 / Topoisomerase I; domain 4 / Topoisomerase I, domain 4 / Topoisomerase (Topo) IA-type catalytic domain profile. / Anthopleurin-A / DNA topoisomerase, type IA, domain 2 / DNA topoisomerase, type IA, DNA-binding domain / DNA topoisomerase, type IA, central / DNA topoisomerase, type IA, central region, subdomain 1 / DNA topoisomerase, type IA, central region, subdomain 3 / DNA topoisomerase, type IA, core domain / DNA topoisomerase / Bacterial DNA topoisomeraes I ATP-binding domain / Bacterial DNA topoisomerase I DNA-binding domain / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 / TOPRIM / Toprim domain / Toprim domain profile. / TOPRIM domain / Single Sheet / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleotide triphosphate hydrolases / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta 類似検索 - ドメイン・相同性
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
CHAIN B ENGINEERED MUTATION PRO719LEU, LEU1046MET. NINETEEN RESIDUES N-TERMINAL TO SERINE 33 IN THE ...CHAIN B ENGINEERED MUTATION PRO719LEU, LEU1046MET. NINETEEN RESIDUES N-TERMINAL TO SERINE 33 IN THE COORDINATES HAVE BEEN MODELLED AS THREE NON-CONTIGUOUS CHAINS OF POLYALANINE. AMINO ACID SEQUENCE AND NUMBERING FOR THESE RESIDUES HAS BEEN ASSIGNED AS 1-21. THEIR ACTUAL POSITION IN THE PROTEIN SEQUENCE IS UNCLEAR DUE TO POOR ELECTRON DENSITY.
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.9686 Å / 相対比: 1
反射
解像度: 2.7→41 Å / Num. obs: 28735 / % possible obs: 99.3 % / 冗長度: 3.2 % / Biso Wilson estimate: 67.6 Å2 / Rsym value: 0.062 / Net I/σ(I): 8.6
反射 シェル
解像度: 2.7→2.78 Å / 冗長度: 3 % / Mean I/σ(I) obs: 2.6 / Rsym value: 0.288 / % possible all: 99.3
反射
*PLUS
最低解像度: 41 Å / Rmerge(I) obs: 0.062
反射 シェル
*PLUS
% possible obs: 99.3 % / Rmerge(I) obs: 0.288
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解析
ソフトウェア
名称
バージョン
分類
CNS
1
精密化
MOSFLM
データ削減
SCALA
データスケーリング
SOLVE/RESOLVE
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.7→41 Å / Data cutoff high absF: 10000 / 交差検証法: THROUGHOUT / σ(F): 0 / 立体化学のターゲット値: MLF 詳細: NINETEEN RESIDUES N-TERMINAL TO SERINE 33 IN THE COORDINATES HAVE BEEN MODELLED AS THREE NON- CONTIGUOUS CHAINS OF POLYALANINE. AMINO ACID SEQUENCE AND NUMBERING FOR THESE RESIDUES HAS BEEN ...詳細: NINETEEN RESIDUES N-TERMINAL TO SERINE 33 IN THE COORDINATES HAVE BEEN MODELLED AS THREE NON- CONTIGUOUS CHAINS OF POLYALANINE. AMINO ACID SEQUENCE AND NUMBERING FOR THESE RESIDUES HAS BEEN ASSIGNED AS 1-21. THEIR ACTUAL POSITION IN THE PROTEIN SEQUENCE IS UNCLEAR DUE TO POOR ELECTRON DENSITY.