+Open data
-Basic information
Entry | Database: PDB / ID: 1aos | ||||||
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Title | HUMAN ARGININOSUCCINATE LYASE | ||||||
Components | ARGININOSUCCINATE LYASE | ||||||
Keywords | LYASE / ARGININE BIOSYNTHESIS / UREA CYCLE | ||||||
Function / homology | Function and homology information ammonia assimilation cycle / argininosuccinate lyase / argininosuccinate lyase activity / arginine metabolic process / Urea cycle / arginine biosynthetic process via ornithine / urea cycle / arginine biosynthetic process / post-embryonic development / locomotory behavior ...ammonia assimilation cycle / argininosuccinate lyase / argininosuccinate lyase activity / arginine metabolic process / Urea cycle / arginine biosynthetic process via ornithine / urea cycle / arginine biosynthetic process / post-embryonic development / locomotory behavior / positive regulation of nitric oxide biosynthetic process / extracellular exosome / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 4.2 Å | ||||||
Authors | Turner, M.A. / Simpson, A. / Mcinnes, R.R. / Howell, P.L. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Human argininosuccinate lyase: a structural basis for intragenic complementation. Authors: Turner, M.A. / Simpson, A. / McInnes, R.R. / Howell, P.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1aos.cif.gz | 153.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1aos.ent.gz | 118.8 KB | Display | PDB format |
PDBx/mmJSON format | 1aos.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1aos_validation.pdf.gz | 428.4 KB | Display | wwPDB validaton report |
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Full document | 1aos_full_validation.pdf.gz | 458.6 KB | Display | |
Data in XML | 1aos_validation.xml.gz | 29.9 KB | Display | |
Data in CIF | 1aos_validation.cif.gz | 41.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ao/1aos ftp://data.pdbj.org/pub/pdb/validation_reports/ao/1aos | HTTPS FTP |
-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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.2466, 0.7165, -0.6525), Vector: |
-Components
#1: Protein | Mass: 51976.176 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOPLASM / Organ: LIVER / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P04424, argininosuccinate lyase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 43 % | |||||||||||||||||||||||||
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Crystal grow | pH: 7.1 / Details: PROTEIN CRYSTALLIZED FROM 1.1M PHOSPHATE, pH 7.1 | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jun 1, 1994 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 4→15 Å / Num. obs: 23049 / % possible obs: 92.3 % / Observed criterion σ(I): 2 / Redundancy: 2.66 % / Rsym value: 0.116 |
Reflection | *PLUS Num. obs: 8659 / Num. measured all: 23049 / Rmerge(I) obs: 0.116 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 4.2→8 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 20.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.2→8 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 4.2→4.36 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.16 |