+
Open data
-
Basic information
Entry | Database: PDB / ID: 1mah | ||||||
---|---|---|---|---|---|---|---|
Title | FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX | ||||||
![]() |
| ||||||
![]() | COMPLEX (HYDROLASE/TOXIN) / ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() acetylcholine metabolic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Bourne, Y. / Taylor, P. / Marchot, P. | ||||||
![]() | ![]() Title: Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Authors: Bourne, Y. / Taylor, P. / Marchot, P. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 112.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 92.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
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 A 106 2: ARG A 107 - PRO A 108 OMEGA = 243.30 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: LEU A 161 - PRO A 162 OMEGA = 222.75 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: SER A 497 - PRO A 498 OMEGA = 139.38 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: CIS PROLINE - PRO F 31 / 6: CIS PROLINE - PRO F 56 | ||||||||
Details | SYMMETRY THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE. APPLIED TO RESIDUES: A 4 .. 61 GENERATE A DIMER OF THE MACHE-FAS2 COMPLEX ACROSS A TWO-FOLD CRYSTALLOGRAPHIC AXIS SYMMETRY1 1 -1.000000 0.000000 0.000000 75.46878 SYMMETRY2 1 0.000000 1.000000 0.000000 -0.07648 SYMMETRY3 1 0.000000 0.000000 -1.000000 278.07110 |
-
Components
#1: Protein | ![]() Mass: 59764.488 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
---|---|
#2: Protein | ![]() Mass: 6768.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Cell line: 293 / Organ: BRAIN (CDNA) / Tissue: VENOM ![]() |
#3: Sugar | ChemComp-NAG / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.44 Å3/Da / Density % sol: 64.21 % |
---|---|
Crystal grow![]() | Details: DATA SETS FROM FOUR CRYSTALS HAVE BEEN MERGED |
Crystal | *PLUS Density % sol: 60 % |
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 7.5 / PH range high: 6.5 |
Components of the solutions | *PLUS Conc.: 0.1 M / Chemical formula: NaAc |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 25, 1995 | |||||||||
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
| |||||||||
Reflection | Resolution: 3.2→37 Å / Num. obs: 14488 / % possible obs: 85 % / Redundancy: 4 % / Rmerge(I) obs: 0.089 | |||||||||
Reflection | *PLUS Num. measured all: 62214 / Rmerge(I) obs: 0.089 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 3.2→10 Å / σ(F): 0
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|