+
Open data
-
Basic information
Entry | Database: PDB / ID: 1iit | ||||||
---|---|---|---|---|---|---|---|
Title | GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE | ||||||
![]() | Slr1257 protein | ||||||
![]() | MEMBRANE PROTEIN / SAME FOLD AS PBPS | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mayer, M.L. / Olson, R. / Gouaux, E. | ||||||
![]() | ![]() Title: Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state. Authors: Mayer, M.L. / Olson, R. / Gouaux, E. #1: ![]() Title: FUNCTIONAL CHARACTERIZATION OF A POTASSIUM-SELECTIVE PROKARYOTIC GLUTAMATE RECEPTOR Authors: CHEN, G.-Q. / CUI, C. / MAYER, M.L. / GOUAUX, E. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE NATIVE GLURO IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED BY THE AUTHOR IS THE ...SEQUENCE NATIVE GLURO IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED BY THE AUTHOR IS THE EXTRACELLULAR LIGAND BINDING DOMAIN OF GLURO. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A THR LINKER. THE SEQUENCE, AS A RESULT, MATCHES DISCONTINUOUSLY WITH THE REFERENCE DATABASE. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 56.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 40 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 25565.977 Da / Num. of mol.: 1 Fragment: GLUR0 LIGAND BINDING CORE, RESIDUES 44-140, 256-385 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: PCC6803 / Gene: slr1257, slr1257 GluR0 / Plasmid: pETGQ / Species (production host): Escherichia coli / Production host: ![]() ![]() |
---|---|
#2: Chemical | ChemComp-SER / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.77 % | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.7 Details: 38% MPD, 0.2 M LiCl, 0.1 M Na Acetate, 10 mM L-Serine, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / PH range low: 4.8 / PH range high: 4.7 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 110 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 17, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97625 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 18810 / % possible obs: 99.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 7 % / Biso Wilson estimate: 20.29 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 27.2 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 6.69 % / Rmerge(I) obs: 0.094 / Mean I/σ(I) obs: 19.3 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 131611 |
Reflection shell | *PLUS % possible obs: 100 % |
-
Processing
Software |
| |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| |||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
| |||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.9→1.99 Å
| |||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | |||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 2 / Rfactor obs: 0.209 / Rfactor Rfree: 0.25 | |||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| |||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.325 / Rfactor Rwork: 0.295 |