+Open data
-Basic information
Entry | Database: PDB / ID: 1atn | |||||||||
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Title | Atomic structure of the actin:DNASE I complex | |||||||||
Components |
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Keywords | ENDODEOXYRIBONUCLEASE | |||||||||
Function / homology | Function and homology information Striated Muscle Contraction / regulation of neutrophil mediated cytotoxicity / regulation of acute inflammatory response / zymogen granule / deoxyribonuclease I / dynactin complex / deoxyribonuclease I activity / neutrophil activation involved in immune response / DNA catabolic process / cytoskeletal motor activator activity ...Striated Muscle Contraction / regulation of neutrophil mediated cytotoxicity / regulation of acute inflammatory response / zymogen granule / deoxyribonuclease I / dynactin complex / deoxyribonuclease I activity / neutrophil activation involved in immune response / DNA catabolic process / cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / actin filament bundle assembly / skeletal muscle thin filament assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / nuclear envelope / actin binding / cell body / hydrolase activity / protein domain specific binding / apoptotic process / calcium ion binding / positive regulation of gene expression / magnesium ion binding / DNA binding / extracellular region / ATP binding / nucleus / identical protein binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | |||||||||
Authors | Kabsch, W. / Mannherz, H.G. / Suck, D. / Pai, E. / Holmes, K.C. | |||||||||
Citation | Journal: Nature / Year: 1990 Title: Atomic structure of the actin:DNase I complex. Authors: Kabsch, W. / Mannherz, H.G. / Suck, D. / Pai, E.F. / Holmes, K.C. #1: Journal: Annu.Rev.Biophys.Biophys.Chem. / Year: 1992 Title: Structure and Function of Actin Authors: Kabsch, W. / Vandekerckhove, J. #2: Journal: Curr.Opin.Struct.Biol. / Year: 1991 Title: Muscle Proteins: Actin Authors: Holmes, K.C. / Kabsch, W. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1991 Title: Similarity of the Three-Dimensional Structures of Actin and the ATPase Fragment of a 70-kDa Heat Shock Cognate Protein Authors: Flaherty, K.M. / Mckay, D.B. / Kabsch, W. / Holmes, K.C. #4: Journal: Nature / Year: 1990 Title: Atomic Model of the Actin Filament Authors: Holmes, K.C. / Popp, D. / Gebhard, W. / Kabsch, W. #5: Journal: J.Mol.Biol. / Year: 1986 Title: Crystallographic Refinement and Structure of DNase I at 2 Angstroms Resolution Authors: Oefner, C. / Suck, D. #6: Journal: Embo J. / Year: 1985 Title: Three-Dimensional Structure of the Complex of Actin and DNase I at 4.5 Angstroms Resolution Authors: Kabsch, W. / Mannherz, H.G. / Suck, D. #7: Journal: Embo J. / Year: 1984 Title: Three-Dimensional Structure of Bovine Pancreatic DNase I at 2.5 Angstroms Resolution Authors: Suck, D. / Oefner, C. / Kabsch, W. #8: Journal: Proc.Natl.Acad.Sci.USA / Year: 1981 Title: Three-Dimensional Structure of the Complex of Skeletal Muscle Actin and Bovine Pancreatic DNase I at 6-Angstroms Resolution Authors: Suck, D. / Kabsch, W. / Mannherz, H.G. | |||||||||
History |
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Remark 700 | SHEET SHEETS A4A AND A4B ARE IDENTICAL EXCEPT FOR THE FIRST STRAND. THIS STRAND IS SPLIT INTO TWO ...SHEET SHEETS A4A AND A4B ARE IDENTICAL EXCEPT FOR THE FIRST STRAND. THIS STRAND IS SPLIT INTO TWO DISTINCT AMINO ACID RUNS. THE BULGE OF 5 AMINO ACIDS INCLUDES HELIX 7. SHEET D1B IS AN EXTENSION OF SHEET D1A. STRANDS 1 TO 4 OF D1B ARE AN EXTENSION OF STRANDS 2 TO 5 OF D1A. SHEETS D2A AND D2B ARE IDENTICAL EXCEPT FOR THE FIRST STRAND. THIS STRAND IS INTERRUPTED BY ONE BULGE RESIDUE. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1atn.cif.gz | 136.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1atn.ent.gz | 107.6 KB | Display | PDB format |
PDBx/mmJSON format | 1atn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/at/1atn ftp://data.pdbj.org/pub/pdb/validation_reports/at/1atn | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE HIS A 73 IS A METHYLATED HISTIDINE. |
-Components
#1: Protein | Mass: 41522.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Organ: PANCREAS / Tissue: MUSCLESkeletal muscle / References: UniProt: P02568, UniProt: P68135*PLUS | ||||
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#2: Protein | Mass: 29047.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: PANCREAS / Tissue: MUSCLESkeletal muscle / References: UniProt: P00639 | ||||
#3: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
#4: Chemical | ChemComp-CA / #5: Chemical | ChemComp-ATP / | Nonpolymer details | THERE IS A CARBOHYDRATE MOIETY CONSISTING OF TWO N-ACETYLGLUCOSAMINE AND 5 MANNOSE RESIDUES WHICH ...THERE IS A CARBOHYDRA | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.69 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.6 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. all: 32996 / Num. obs: 31362 / % possible obs: 81 % / Observed criterion σ(I): 1 / Num. measured all: 103367 / Rmerge(I) obs: 0.107 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2.8→10 Å / Rfactor Rwork: 0.21 / σ(I): 1 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 10 Å / Rfactor obs: 0.21 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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