[English] 日本語
![](img/lk-miru.gif)
- PDB-1mal: STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANN... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1mal | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION | ||||||
![]() | MALTOPORIN | ||||||
![]() | OUTER MEMBRANE PROTEIN | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schirmer, T. | ||||||
![]() | ![]() 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. #1: ![]() Title: Crystallization and Preliminary X-Ray Characterization of Maltoporin from E.Coli Authors: Stauffer, K.A. / Page, M.P.G. / Hardmeyer, A. / Keller, T.A. / Pauptit, R.A. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY A EIGHTEEN-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY A EIGHTEEN-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINETEEN-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THERE IS A BETA-BULGE IN STRAND 6 (RESIDUES 131 - 132) AND IN STRAND 8 (RESIDUES 177 - 178). |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 247.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 209.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 388.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 431.1 KB | Display | |
Data in XML | ![]() | 29.6 KB | Display | |
Data in CIF | ![]() | 44.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
| ||||||||||||
Atom site foot note | 1: CIS PROLINE - PRO 361 | ||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-
Components
#1: Protein | Mass: 47425.785 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 5.48 Å3/Da / Density % sol: 77.56 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Detector | Date: Jan 7, 1994 |
---|---|
Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3.1→8 Å / Num. obs: 51039 / % possible obs: 95.5 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.088 |
Reflection | *PLUS Rmerge(I) obs: 0.088 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 3.1→8 Å / σ(F): 0 Details: ATOMS THAT ARE NOT DEFINED BY ELECTRON-DENSITY HAVE BEEN ASSIGNED AN OCCUPANCY OF 0.0. RESIDUE ASP 78 IS CLOSE TO THE LOCAL THREE-FOLD AXIS; INTERACTIONS WITH ITS LOCAL SYMMETRY MATES ARE ...Details: ATOMS THAT ARE NOT DEFINED BY ELECTRON-DENSITY HAVE BEEN ASSIGNED AN OCCUPANCY OF 0.0. RESIDUE ASP 78 IS CLOSE TO THE LOCAL THREE-FOLD AXIS; INTERACTIONS WITH ITS LOCAL SYMMETRY MATES ARE MEDIATED BY AN UNMODELED ATOM OR MOLECULE (PROBABLY A CATION) THAT IS LOCATED ON THE THREE-FOLD AXIS AS JUDGED BY THE APPARENT STRONG ELECTRON DENSITY.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|