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Open data
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Basic information
Entry | Database: PDB / ID: 1pdo | ||||||
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Title | PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM | ||||||
![]() | MANNOSE PERMEASE | ||||||
![]() | PHOSPHOTRANSFERASE / PHOSPHOENOLPYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM | ||||||
Function / homology | ![]() protein-Npi-phosphohistidine-D-mannose phosphotransferase / mannose transmembrane transport / protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity / glucose import across plasma membrane / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / phosphorylation / protein homodimerization activity / membrane ...protein-Npi-phosphohistidine-D-mannose phosphotransferase / mannose transmembrane transport / protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity / glucose import across plasma membrane / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / phosphorylation / protein homodimerization activity / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nunn, R.S. / Erni, B. / Schirmer, T. | ||||||
![]() | ![]() Title: Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution. Authors: Nunn, R.S. / Markovic-Housley, Z. / Genovesio-Taverne, J.C. / Flukiger, K. / Rizkallah, P.J. / Jansonius, J.N. / Schirmer, T. / Erni, B. #1: ![]() Title: The Mannose Permease of Escherichia Coli Consists of Three Different Proteins. Amino Acid Sequence and Function in Sugar Transport, Sugar Phosphorylation, and Penetration of Phage Lambda DNA Authors: Erni, B. / Zanolari, B. / Kocher, H.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 38.2 KB | Display | ![]() |
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PDB format | ![]() | 26.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408.5 KB | Display | ![]() |
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Full document | ![]() | 409.4 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 9.7 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 14624.625 Da / Num. of mol.: 1 Fragment: IIA ==MAN== DOMAIN, RESIDUES 2 - 133, OF THE IIAB ==MAN== SUBUNIT PLUS PHE-ALA-GLY AT THE CARBOXY TERMINUS Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: SUBCLONAL IIA COMPRISES RESIDUES 1 - 133 OF THE WILD-TYPE IIAB SEQUENCE PLUS PHE-ALA-GLY AT THE CARBOXY TERMINUS. THE INITIAL SE-MET WAS REMOVED BY PROTEOLYTIC CLEAVAGE. Plasmid: PJFL1320 / Species (production host): Escherichia coli / Gene (production host): MANX / Production host: ![]() ![]() References: UniProt: P69797, protein-Npi-phosphohistidine-sugar phosphotransferase |
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#2: Water | ChemComp-HOH / |
Compound details | DURING CATALYSIS HIS 10 GETS TRANSIENTL |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 46 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.8 / Details: pH 6.8 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 3, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→19.8 Å / Num. obs: 16839 / % possible obs: 97.3 % / Observed criterion σ(I): 4 / Redundancy: 5.9 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 32.4 |
Reflection shell | Resolution: 1.7→1.74 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.272 / Mean I/σ(I) obs: 8.1 / % possible all: 95.8 |
Reflection shell | *PLUS % possible obs: 95.8 % |
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Processing
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Refinement | Method to determine structure: MIRAS SOFTWARE USED : CCP4 PROGRAM SUITE 1994 STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL Resolution: 1.7→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 20.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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