+Open data
-Basic information
Entry | Database: PDB / ID: 1mpq | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | MALTOPORIN TREHALOSE COMPLEX | |||||||||
Components | MALTOPORIN | |||||||||
Keywords | MEMBRANE PROTEIN / SPECIFIC PORIN / BETA BARREL / SUGAR TRANSPORT | |||||||||
Function / homology | Function and homology information maltodextrin transmembrane transporter activity / maltose transporting porin activity / polysaccharide transport / porin activity / pore complex / carbohydrate transmembrane transporter activity / maltodextrin transmembrane transport / 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 / MOLECULAR REPLACEMENT / Resolution: 3 Å | |||||||||
Authors | Dutzler, R. / Schirmer, T. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. Authors: Wang, Y.F. / Dutzler, R. / Rizkallah, P.J. / Rosenbusch, J.P. / Schirmer, T. #1: 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. / Rosenbusch, J.P. / Schirmer, T. #2: 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1mpq.cif.gz | 251.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1mpq.ent.gz | 206.9 KB | Display | PDB format |
PDBx/mmJSON format | 1mpq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mpq_validation.pdf.gz | 615 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1mpq_full_validation.pdf.gz | 650.9 KB | Display | |
Data in XML | 1mpq_validation.xml.gz | 47.5 KB | Display | |
Data in CIF | 1mpq_validation.cif.gz | 64.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/1mpq ftp://data.pdbj.org/pub/pdb/validation_reports/mp/1mpq | HTTPS FTP |
-Related structure data
Related structure data | 1af6C 1malS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
| ||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-Components
#1: Protein | Mass: 47425.785 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cellular location: OUTER MEMBRANE / Gene: LAMB / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli (E. coli) / References: UniProt: P02943 #2: Polysaccharide | Nonpolymer details | GLC 1 OF TREHALOSE WAS DISORDERED AND THUS MODELED STEREOCHEMICALLY. A SINGLE GROUP B-FACTOR WAS ...GLC 1 OF TREHALOSE WAS DISORDERED | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 5.29 Å3/Da / Density % sol: 75 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7 / Details: pH 7. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-20 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 12, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. obs: 59057 / % possible obs: 97.7 % / Observed criterion σ(I): 4 / Redundancy: 3.3 % / Biso Wilson estimate: 61 Å2 / Rmerge(I) obs: 0.078 |
Reflection shell | Resolution: 3→3.11 Å / Redundancy: 3 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 2.5 / % possible all: 93.2 |
Reflection shell | *PLUS % possible obs: 93.2 % |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MAL Resolution: 3→8 Å / Cross valid method: THROUGHOUT / σ(F): 0
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.1 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: STRICT NCS CONSTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3→3.05 Å / Total num. of bins used: 20
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|