+Open data
-Basic information
Entry | Database: PDB / ID: 2ald | ||||||
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Title | HUMAN MUSCLE ALDOLASE | ||||||
Components | FRUCTOSE-BISPHOSPHATE ALDOLASE | ||||||
Keywords | LYASE / LYASE (ALDEHYDE) / TYPE I ALDOLASE | ||||||
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 / M band / fructose metabolic process / I band ...fructose binding / sperm head / ATP biosynthetic process / fructose-bisphosphate aldolase / binding of sperm to zona pellucida / fructose-bisphosphate aldolase activity / Gluconeogenesis / M band / fructose metabolic process / 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 / glycolytic process / actin filament organization / actin cytoskeleton / tertiary granule lumen / Platelet degranulation / actin binding / regulation of cell shape / protein homotetramerization / secretory granule lumen / 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 / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Dalby, A.R. / Littlechild, J.A. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Authors: Dalby, A. / Dauter, Z. / Littlechild, J.A. #1: 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. #2: Journal: FEBS Lett. / Year: 1990 Title: The Crystal Structure of Human Muscle Aldolase at 3.0 A Resolution Authors: Gamblin, S.J. / Cooper, B. / Millar, J.R. / Davies, G.J. / Littlechild, J.A. / Watson, H.C. #3: Journal: FEBS Lett. / Year: 1990 Title: Erratum. The Crystal Structure of Human Muscle Aldolase at 3.0 A Resolution Authors: Gamblin, S.J. / Cooper, B. / Millar, J.R. / Davies, G.J. / Littlechild, J.A. / Watson, H.C. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1987 Title: Molecular Architecture of Rabbit Skeletal Muscle Aldolase at 2.7-A Resolution Authors: Sygusch, J. / Beaudry, D. / Allaire, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ald.cif.gz | 84 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ald.ent.gz | 63.6 KB | Display | PDB format |
PDBx/mmJSON format | 2ald.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ald_validation.pdf.gz | 368.9 KB | Display | wwPDB validaton report |
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Full document | 2ald_full_validation.pdf.gz | 381.1 KB | Display | |
Data in XML | 2ald_validation.xml.gz | 10 KB | Display | |
Data in CIF | 2ald_validation.cif.gz | 15.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/al/2ald ftp://data.pdbj.org/pub/pdb/validation_reports/al/2ald | HTTPS FTP |
-Related structure data
-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 natural source / Details: LEG TISSUE / Source: (natural) Homo sapiens (human) / Organ: SKELETAL / Tissue: MUSCLE / References: UniProt: P04075, fructose-bisphosphate aldolase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55 % |
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Crystal grow | pH: 7.5 / Details: pH 7.5 |
Crystal grow | *PLUS Method: unknownDetails: Millar, J.R., (1981) Phil. Trans. R. Soc. Lond. B, 293, 209. |
-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.95 |
Detector | Detector: FILM |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→19.68 Å / Num. obs: 21561 / % possible obs: 78.7 % / Observed criterion σ(I): 3 / Redundancy: 4 % / Biso Wilson estimate: 31.3 Å2 / Rmerge(I) obs: 0.06 |
Reflection | *PLUS Highest resolution: 2.1 Å / Rmerge(I) obs: 0.06 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→20 Å / SU B: 4.78 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 29.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.172 / Rfactor obs: 0.162 / Highest resolution: 2.1 Å / Lowest resolution: 19.68 Å / Rfactor Rfree: 0.258 / Rfactor Rwork: 0.162 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |