+Open data
-Basic information
Entry | Database: PDB / ID: 1ald | ||||||
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Title | ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES | ||||||
Components | ALDOLASE A | ||||||
Keywords | LYASE (ALDEHYDE) | ||||||
Function / homology | Function and homology information fructose binding / sperm head / ATP biosynthetic process / fructose-bisphosphate aldolase / binding of sperm to zona pellucida / fructose-bisphosphate aldolase activity / Gluconeogenesis / fructose metabolic process / M band / I band ...fructose binding / sperm head / ATP biosynthetic process / fructose-bisphosphate aldolase / binding of sperm to zona pellucida / fructose-bisphosphate aldolase activity / Gluconeogenesis / fructose metabolic process / M band / I band / fructose 1,6-bisphosphate metabolic process / Glycolysis / muscle cell cellular homeostasis / striated muscle contraction / cytoskeletal protein binding / tubulin binding / platelet alpha granule lumen / actin filament organization / glycolytic process / actin cytoskeleton / tertiary granule lumen / Platelet degranulation / actin binding / regulation of cell shape / secretory granule lumen / protein homotetramerization / ficolin-1-rich granule lumen / cadherin binding / Neutrophil degranulation / RNA binding / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Watson, H.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 Title: Activity and specificity of human aldolases. Authors: Gamblin, S.J. / Davies, G.J. / Grimes, J.M. / Jackson, R.M. / Littlechild, J.A. / Watson, H.C. #1: Journal: FEBS Lett. / Year: 1990 Title: The Crystal Structure of Human Muscle Aldolase at 3.0 Angstroms Resolution Authors: Gamblin, S.J. / Cooper, B. / Millar, J.R. / Davies, G.J. / Littlechild, J.A. / Watson, H.C. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1987 Title: Molecular Architecture of Rabbit Skeletal Muscle Aldolase at 2.7-Angstroms Resolution Authors: Sygusch, J. / Beaudry, D. / Allaire, M. #3: Journal: Philos.Trans.R.Soc.London,Ser.B / Year: 1981 Title: The Low-Resolution Structure of Human Muscle Aldolase Authors: Millar, J.R. / Shaw, P.J. / Stammers, D.K. / Watson, H.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ald.cif.gz | 76.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ald.ent.gz | 59.6 KB | Display | PDB format |
PDBx/mmJSON format | 1ald.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ald_validation.pdf.gz | 365.1 KB | Display | wwPDB validaton report |
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Full document | 1ald_full_validation.pdf.gz | 389.4 KB | Display | |
Data in XML | 1ald_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 1ald_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/al/1ald ftp://data.pdbj.org/pub/pdb/validation_reports/al/1ald | 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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-Components
#1: Protein | Mass: 39338.777 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P04075, fructose-bisphosphate aldolase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.72 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.3 / Method: otherDetails: referred to 'Eagles, P. A.', (1969) J. Mol. Biol., 45, 533-544 | |||||||||||||||||||||||||
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 Å / Num. all: 23815 / Num. obs: 21427 / Observed criterion σ(I): 3 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||
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Refinement | Highest resolution: 2 Å / σ(F): 3
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Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refinement | *PLUS Highest resolution: 2 Å / Rfactor obs: 0.22 / Lowest resolution: 3 Å / Num. reflection obs: 21427 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS |