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Open data
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Basic information
Entry | Database: PDB / ID: 1a3a | ||||||
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Title | CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI | ||||||
![]() | MANNITOL-SPECIFIC EII | ||||||
![]() | PHOSPHOTRANSFERASE / PHOSPHOENOLPYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM / IIA ENZYMES / HISTIDINE PHOSPHORYLATION | ||||||
Function / homology | ![]() 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 / phosphorylation / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Van Montfort, R.L.M. / Pijning, T. / Kalk, K.H. / Hangyi, I. / Kouwijzer, M.L.C.E. / Robillard, G.T. / Dijkstra, B.W. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 130.1 KB | Display | ![]() |
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PDB format | ![]() | 102.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.3 KB | Display | ![]() |
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Full document | ![]() | 437.4 KB | Display | |
Data in XML | ![]() | 28.1 KB | Display | |
Data in CIF | ![]() | 41.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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.) ![]() ![]() ![]() ![]() References: UniProt: P00550, protein-Npi-phosphohistidine-sugar phosphotransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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 % |
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Processing
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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: ![]() | ||||||||||||||||
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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