+Open data
-Basic information
Entry | Database: PDB / ID: 1a3a | ||||||
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Title | CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI | ||||||
Components | MANNITOL-SPECIFIC EII | ||||||
Keywords | PHOSPHOTRANSFERASE / PHOSPHOENOLPYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM / IIA ENZYMES / HISTIDINE PHOSPHORYLATION | ||||||
Function / homology | Function and homology information protein-Npi-phosphohistidine-D-mannitol phosphotransferase / protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity / protein-phosphocysteine-mannitol phosphotransferase system transporter activity / mannitol transmembrane transport / protein-phosphocysteine-sugar phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / kinase activity / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MULTIPLE ANOMALOUS DISPERSION / Resolution: 1.8 Å | ||||||
Authors | Van Montfort, R.L.M. / Pijning, T. / Kalk, K.H. / Hangyi, I. / Kouwijzer, M.L.C.E. / Robillard, G.T. / Dijkstra, B.W. | ||||||
Citation | Journal: Structure / Year: 1998 Title: The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site. Authors: van Montfort, R.L. / Pijning, T. / Kalk, K.H. / Hangyi, I. / Kouwijzer, M.L. / Robillard, G.T. / Dijkstra, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a3a.cif.gz | 130.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a3a.ent.gz | 102.6 KB | Display | PDB format |
PDBx/mmJSON format | 1a3a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a3a_validation.pdf.gz | 434.3 KB | Display | wwPDB validaton report |
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Full document | 1a3a_full_validation.pdf.gz | 437.4 KB | Display | |
Data in XML | 1a3a_validation.xml.gz | 28.1 KB | Display | |
Data in CIF | 1a3a_validation.cif.gz | 41.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a3/1a3a ftp://data.pdbj.org/pub/pdb/validation_reports/a3/1a3a | 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 16348.547 Da / Num. of mol.: 4 / Fragment: IIA DOMAIN, RESIDUES 491 - 637 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Cellular location: CYTOPLASM / Gene: MTLA / Production host: Escherichia coli (E. coli) References: UniProt: P00550, protein-Npi-phosphohistidine-sugar phosphotransferase #2: Water | ChemComp-HOH / | |
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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: 1.9 Å3/Da / Density % sol: 36.4 % Description: MAD DATA WERE COLLECTED AT THE BM14 AT THE ESRF, GRENOBLE | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 5 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.8 Å / Num. obs: 45271 / % possible obs: 95.8 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 1.8→1.83 Å / Rmerge(I) obs: 0.262 / % possible all: 84.2 |
Reflection | *PLUS Num. measured all: 195844 |
Reflection shell | *PLUS % possible obs: 84.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MULTIPLE ANOMALOUS DISPERSION Resolution: 1.8→5 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 1.8→5 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Rfactor all: 0.185 / Rfactor obs: 0.19 / Rfactor Rwork: 0.19 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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