[English] 日本語
![](img/lk-miru.gif)
- PDB-1jje: IMP-1 METALLO BETA-LACTAMASE FROM PSEUDOMONAS AERUGINOSA IN COMPL... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1jje | ||||||
---|---|---|---|---|---|---|---|
Title | IMP-1 METALLO BETA-LACTAMASE FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH A BIARYL SUCCINIC ACID INHIBITOR (11) | ||||||
![]() | IMP-1 METALLO BETA-LACTAMASE | ||||||
![]() | HYDROLASE / METALLO-BETA-LACTAMASE INHIBITOR / SUCCINIC ACID INHIBITOR / IMP-1 METALLO-BETA-LACTAMASE | ||||||
Function / homology | ![]() antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fitzgerald, P.M.D. / Sharma, N. | ||||||
![]() | ![]() Title: Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase. Authors: Toney, J.H. / Hammond, G.G. / Fitzgerald, P.M. / Sharma, N. / Balkovec, J.M. / Rouen, G.P. / Olson, S.H. / Hammond, M.L. / Greenlee, M.L. / Gao, Y.D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 104.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 79.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 24535.006 Da / Num. of mol.: 2 / Fragment: metallo-beta-lactamase Source method: isolated from a genetically manipulated source Details: PLEASE NOTE THAT THE PROTEIN CONTAINS POSTRANSLATIONAL MODIFICATION: ATOM CG OF ASN 26 IS BOUND TO ATOM N OF GLY 27. THIS ACCOUNTS FOR MISSING ATOMS LISTED IN REMARK 470 AND DISTORTED ...Details: PLEASE NOTE THAT THE PROTEIN CONTAINS POSTRANSLATIONAL MODIFICATION: ATOM CG OF ASN 26 IS BOUND TO ATOM N OF GLY 27. THIS ACCOUNTS FOR MISSING ATOMS LISTED IN REMARK 470 AND DISTORTED GEOMETRY REPORTED FOR THESE RESIDUES. Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P52699, UniProt: Q79MP6*PLUS, beta-lactamase #2: Chemical | ChemComp-ZN / #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 38.3 % | ||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 310 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: PEG MONOMETHYL ETHER 550, ZINC ACETATE, MES PH 6.7-7.1, 310 K, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 310K | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 37 ℃ / pH: 7.2 | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 22, 1999 | |||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
| |||||||||
Reflection | Resolution: 1.8→99 Å / Num. all: 35791 / Num. obs: 35791 / % possible obs: 99.7 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.59 % / Biso Wilson estimate: 52.2 Å2 / Rmerge(I) obs: 0.0752 / Net I/σ(I): 13.005 | |||||||||
Reflection shell | Resolution: 1.8→1.91 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.4997 / Mean I/σ(I) obs: 1.336 / Num. unique all: 5910 / % possible all: 100 | |||||||||
Reflection | *PLUS Lowest resolution: 9999 Å | |||||||||
Reflection shell | *PLUS % possible obs: 100 % / Num. unique obs: 5910 |
-
Processing
Software |
| |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: ANOTHER INHIBITED COMPLEX IN THE SAME SPACE GROUP Resolution: 1.8→10 Å / Num. parameters: 14767 / Num. restraintsaints: 14533 / Cross valid method: THROUGHOUT / σ(F): -3 / σ(I): -3 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||||
Solvent computation | Solvent model: SHELXL 97 SWAT PARAMETER REFINEMENT | |||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.2 Å2 | |||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 3688 | |||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
| |||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||
Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||
Refinement | *PLUS σ(F): -3 / % reflection Rfree: 5 % | |||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_plane_restr / Dev ideal: 0.337 | |||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.87 Å / Num. reflection obs: 3653 / Rfactor obs: 0.365 |