+Open data
-Basic information
Entry | Database: PDB / ID: 1mpo | |||||||||
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Title | MALTOPORIN MALTOHEXAOSE COMPLEX | |||||||||
Components | MALTOPORIN | |||||||||
Keywords | MEMBRANE PROTEIN / SPECIFIC PORIN / BETA BARREL MEMBRANE PROTEIN / SUGAR TRANSPORT / BETA BARREL | |||||||||
Function / homology | Function and homology information maltodextrin transmembrane transporter activity / maltose transporting porin activity / polysaccharide transport / porin activity / pore complex / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / monoatomic ion transport / cell outer membrane / virus receptor activity / DNA damage response Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.8 Å | |||||||||
Authors | Dutzler, R. / Schirmer, T. | |||||||||
Citation | Journal: Structure / Year: 1996 Title: Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Authors: Dutzler, R. / Wang, Y.F. / Rizkallah, P.J. / Rosenbusch, J.P. / Schirmer, T. #1: Journal: Science / Year: 1995 Title: Structural Basis for Sugar Translocation Through Maltoporin Channels at 3.1 A Resolution Authors: Schirmer, T. / Keller, T.A. / Wang, Y.F. / Rosenbusch, J.P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mpo.cif.gz | 261.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mpo.ent.gz | 216.7 KB | Display | PDB format |
PDBx/mmJSON format | 1mpo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/1mpo ftp://data.pdbj.org/pub/pdb/validation_reports/mp/1mpo | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THE ASYMMETRIC UNIT CONTAINS THREE MONOMERS A, B, AND C. CHAINS B AND C OF THE ENTRY HAVE BEEN GENERATED BY THE PDB TO PROVIDE THE OTHER TWO SUBUNITS OF THE MOLECULAR THREE-FOLD TRIMER. |
-Components
#1: Protein | Mass: 47425.785 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P02943 #2: Polysaccharide | #3: Chemical | #4: Water | ChemComp-HOH / | Nonpolymer details | MALTOHEXAOSE CONSISTS OF SIX ALPHA-1 - 4 LINKED GLUCOSYL RESIDUES. THE ELECTRON DENSITY THAT ...MALTOHEXAO | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density % sol: 75 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 0.96 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 2, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.96 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 68475 / % possible obs: 94.3 % / Observed criterion σ(I): 4 / Redundancy: 3 % / Rmerge(I) obs: 0.083 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å / % possible obs: 95.3 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.37 |
-Processing
Software |
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Refinement | Resolution: 2.8→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 43 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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