+Open data
-Basic information
Entry | Database: PDB / ID: 1mah | ||||||
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Title | FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX | ||||||
Components |
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Keywords | COMPLEX (HYDROLASE/TOXIN) / HYDROLASE / SERINE ESTERASE / SYNAPSE / VENOM / TOXIN / COMPLEX (HYDROLASE-TOXIN) COMPLEX | ||||||
Function / homology | Function and homology information acetylcholine metabolic process / serine hydrolase activity / choline binding / acetylcholine catabolic process / acetylcholine binding / acetylcholinesterase / positive regulation of dendrite morphogenesis / acetylcholine receptor signaling pathway / choline metabolic process / osteoblast development ...acetylcholine metabolic process / serine hydrolase activity / choline binding / acetylcholine catabolic process / acetylcholine binding / acetylcholinesterase / positive regulation of dendrite morphogenesis / acetylcholine receptor signaling pathway / choline metabolic process / osteoblast development / acetylcholinesterase activity / positive regulation of axonogenesis / basement membrane / regulation of receptor recycling / synaptic cleft / side of membrane / laminin binding / collagen binding / synapse assembly / response to insulin / neuromuscular junction / receptor internalization / positive regulation of cold-induced thermogenesis / nuclear envelope / retina development in camera-type eye / presynaptic membrane / toxin activity / postsynaptic membrane / cell adhesion / endoplasmic reticulum lumen / axon / neuronal cell body / dendrite / synapse / perinuclear region of cytoplasm / Golgi apparatus / cell surface / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Dendroaspis angusticeps (eastern green mamba) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.2 Å | ||||||
Authors | Bourne, Y. / Taylor, P. / Marchot, P. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1995 Title: Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Authors: Bourne, Y. / Taylor, P. / Marchot, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mah.cif.gz | 112.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mah.ent.gz | 92.4 KB | Display | PDB format |
PDBx/mmJSON format | 1mah.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mah_validation.pdf.gz | 395.7 KB | Display | wwPDB validaton report |
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Full document | 1mah_full_validation.pdf.gz | 414.6 KB | Display | |
Data in XML | 1mah_validation.xml.gz | 14.7 KB | Display | |
Data in CIF | 1mah_validation.cif.gz | 22 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ma/1mah ftp://data.pdbj.org/pub/pdb/validation_reports/ma/1mah | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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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.) Mus musculus (house mouse) / Strain: BLACK6-CBA CROSS F1 / Cell line: 293 / Gene: MOUSE ACHE / Organ: BRAIN (CDNA) / Plasmid: LAMBDA-ZAP AND LAMBDA-FIX CDNA AND GENOMIC DNA / Cell line (production host): HEK 293 / Gene (production host): MOUSE ACHE / Production host: Homo sapiens (human) / References: UniProt: P21836, acetylcholinesterase |
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#2: Protein | Mass: 6768.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Dendroaspis angusticeps (eastern green mamba) Cell line: 293 / Organ: BRAIN (CDNA) / Tissue: VENOM / References: UniProt: P01403, UniProt: P0C1Z0*PLUS |
#3: Sugar | ChemComp-NAG / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.44 Å3/Da / Density % sol: 64.21 % |
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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: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 1.0, 1.5 | |||||||||
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 25, 1995 | |||||||||
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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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 |
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Refinement | Resolution: 3.2→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→10 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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