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- PDB-5heh: Pentameric ligand-gated ion channel GLIC mutant P246A -

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Basic information

Entry
Database: PDB / ID: 5heh
TitlePentameric ligand-gated ion channel GLIC mutant P246A
ComponentsProton-gated ion channel
KeywordsTRANSPORT PROTEIN / Pentameric ligand-gated ion channels / Membrane protein / Ligand-gated ion channel
Function / homology
Function and homology information


sodium channel activity / extracellular ligand-gated monoatomic ion channel activity / transmembrane transporter complex / potassium channel activity / regulation of membrane potential / transmembrane signaling receptor activity / neuron projection / signal transduction / identical protein binding / plasma membrane
Similarity search - Function
Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain ...Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Distorted Sandwich / Up-down Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Proton-gated ion channel
Similarity search - Component
Biological speciesGloeobacter violaceus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsBertozzi, C. / Dutzler, R.
CitationJournal: Plos Biol. / Year: 2016
Title: Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels.
Authors: Bertozzi, C. / Zimmermann, I. / Engeler, S. / Hilf, R.J. / Dutzler, R.
History
DepositionJan 6, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Mar 2, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 16, 2016Group: Database references
Revision 1.2Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proton-gated ion channel
B: Proton-gated ion channel
C: Proton-gated ion channel
D: Proton-gated ion channel
E: Proton-gated ion channel


Theoretical massNumber of molelcules
Total (without water)180,9735
Polymers180,9735
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21280 Å2
ΔGint-145 kcal/mol
Surface area65680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)177.690, 133.940, 159.830
Angle α, β, γ (deg.)90.00, 101.10, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
Proton-gated ion channel / GLIC / Ligand-gated ion channel / LGIC


Mass: 36194.637 Da / Num. of mol.: 5 / Mutation: P246A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gloeobacter violaceus (bacteria) / Gene: glvI, glr4197 / Production host: Escherichia coli (E. coli) / References: UniProt: Q7NDN8

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 5.16 Å3/Da / Density % sol: 76.15 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 4 / Details: PEG 4000, Ammonium Sulfate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9197 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 28, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9197 Å / Relative weight: 1
ReflectionResolution: 3.3→50 Å / Num. obs: 55197 / % possible obs: 99.6 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.101 / Net I/σ(I): 13.1
Reflection shellResolution: 3.3→3.4 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.773 / Mean I/σ(I) obs: 2.4 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(1.10_2155: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3EHZ
Resolution: 3.3→29.913 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.02 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2803 2794 5.07 %
Rwork0.2438 --
obs0.2457 55058 99.5 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.3→29.913 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12595 0 0 0 12595
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00312930
X-RAY DIFFRACTIONf_angle_d0.65417660
X-RAY DIFFRACTIONf_dihedral_angle_d15.1287640
X-RAY DIFFRACTIONf_chiral_restr0.0432060
X-RAY DIFFRACTIONf_plane_restr0.0042210
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3-3.35680.39961870.35822559X-RAY DIFFRACTION100
3.3568-3.41780.40561000.34642644X-RAY DIFFRACTION100
3.4178-3.48340.3943960.33462657X-RAY DIFFRACTION99
3.4834-3.55440.35151780.31342517X-RAY DIFFRACTION100
3.5544-3.63160.33591810.30022562X-RAY DIFFRACTION99
3.6316-3.71590.32211020.29332675X-RAY DIFFRACTION100
3.7159-3.80870.3232840.26772643X-RAY DIFFRACTION100
3.8087-3.91140.35671870.27042541X-RAY DIFFRACTION100
3.9114-4.02630.33951870.27172578X-RAY DIFFRACTION100
4.0263-4.15590.3254690.24892677X-RAY DIFFRACTION100
4.1559-4.3040.29381180.2422638X-RAY DIFFRACTION100
4.304-4.47580.29051870.22292575X-RAY DIFFRACTION100
4.4758-4.67880.20581870.19292554X-RAY DIFFRACTION100
4.6788-4.92440.2815500.17842693X-RAY DIFFRACTION100
4.9244-5.23140.24211360.19022637X-RAY DIFFRACTION100
5.2314-5.63290.25071870.23762581X-RAY DIFFRACTION100
5.6329-6.19520.30711870.25252566X-RAY DIFFRACTION99
6.1952-7.08120.273860.2432758X-RAY DIFFRACTION100
7.0812-8.88270.30931810.2182584X-RAY DIFFRACTION99
8.8827-29.91390.19691840.2352625X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.6101-0.2731-0.41980.01750.25050.1622-0.16530.12490.44860.067-0.28590.317-0.00020.2013-0.01230.7766-0.09810.06820.5389-0.02940.412921.0313-4.452584.5042
20.52760.29760.11841.2355-0.02910.40420.2297-0.1328-0.26140.32260.0365-0.06150.1762-0.3194-0.00030.429-0.04120.02680.4921-0.00070.47298.6017-7.480556.7556
30.0798-0.35-0.07880.14420.09340.09320.14030.095-0.3483-0.2841-0.05290.3678-0.3036-0.7821-00.631-0.00610.00250.8319-0.08320.6444-3.5135-12.491829.0276
40.2201-0.04460.25570.3865-0.09460.1619-0.0391-0.17980.09130.3192-0.27620.042-0.01920.078800.58650.10170.16480.5781-0.03350.469822.139219.46775.9884
50.0558-0.0629-0.02780.05070.00530.0439-0.0994-0.4361-0.19550.68070.64910.08850.03440.31360.00021.27270.1787-0.34371.2356-0.21830.851535.134628.600897.808
60.1868-0.0156-0.00690.0249-0.07040.0786-0.47480.016-0.01230.58120.3142-0.00830.19090.7002-0.00010.74040.10920.03680.7063-0.12790.531328.725617.669680.8124
70.4022-0.40430.05410.36460.25360.4743-0.3864-0.31790.2435-0.0788-0.3087-0.1343-0.4446-0.347-0.02920.5129-0.0651-0.03410.37950.00990.459115.502320.767269.6739
80.2711-0.1549-0.08680.15940.17110.17260.107-0.32560.1812-0.4232-0.1947-0.14480.0332-0.34550.00010.9288-0.1784-0.0980.80910.04680.642312.284319.099875.435
90.14990.0080.01080.34830.13910.0496-0.0909-0.0107-0.3208-0.19860.48240.28640.3353-0.1620.38671.4415-0.5895-0.442-0.037-0.02560.651613.295221.50359.6379
100.47130.0354-0.63380.3806-0.0150.6134-0.23190.07010.04370.1654-0.048-0.1579-0.1542-0.069700.6347-0.0096-0.05780.69810.01740.68120.907210.681831.062
110.1220.3288-0.15530.4437-0.3130.172-0.03560.4798-0.2499-0.60530.19310.71590.4101-0.58510.02140.64330.5332-0.04631.1357-0.40730.8486-8.176719.523833.5576
120.5588-0.19110.09070.0463-0.04850.03160.0064-0.27890.408-0.1256-0.12930.16840.3377-0.1253-0.00010.5722-0.1272-0.12170.58840.00350.640645.094723.171163.9322
130.3896-0.27110.03390.2111-0.06760.119-0.1555-0.22480.13730.10830.13260.0283-0.553-0.04930.00111.10150.5682-0.62811.438-0.63631.605364.858824.752682.2113
140.0556-0.2001-0.07360.29160.31310.14890.1809-0.13280.1991-0.3211-0.0259-0.02280.2737-0.2248-0.00010.69830.104-0.19730.5376-0.10840.718147.936619.239370.7444
152.17-0.6186-1.10710.26080.69751.6224-0.70270.64111.09920.3115-0.3573-0.6627-1.0168-0.1347-0.8040.3748-0.3048-0.0444-0.2440.20250.522641.392126.345356.0858
160.1508-0.08390.16190.3356-0.15010.1584-0.22010.05720.0398-0.28550.08810.0059-0.0428-0.017400.8628-0.150.04140.58870.03440.638740.128331.104460.7687
170.0480.02810.1298-0.02950.10760.12920.05840.0509-0.15240.03480.0342-0.2103-0.37420.09450.3264-0.21150.00780.83730.6446-0.10360.078838.14523.952246.603
180.6430.1518-0.41480.724-0.16080.2561-0.10140.51920.0935-0.5909-0.16180.272-0.53870.2315-0.00310.65470.0011-0.05170.74860.10060.608115.312118.350923.5055
190.993-0.415-0.98060.16250.40660.99270.574-0.0877-0.0671-2.01430.79120.95850.4254-0.11160.76971.4541-0.1289-0.63630.79330.26310.893919.337929.822919.0903
200.3792-0.1773-0.2357-0.16550.08820.6307-0.05570.091-0.1495-0.11120.00910.1145-0.0996-0.3236-00.4460.003-0.06540.4431-0.02790.526257.0077-2.217465.8858
210.5161-0.10790.3745-0.56190.08740.16970.40840.42390.0374-0.556-0.18880.0830.28990.3953-0.00590.61340.0299-0.05020.54-0.00330.584243.74011.287938.6044
220.3340.0821-0.35280.0958-0.04160.3421-0.20550.5563-0.0155-0.27160.00090.0502-0.23610.5398-0.00010.6345-0.05320.04710.80190.02640.519931.38236.534311.007
230.01410.09630.10140.0743-0.02850.5946-0.1742-0.39540.10950.0159-0.12190.0692-0.2311-0.5192-0.00570.6844-0.0697-0.09690.37360.05380.465138.2118-18.796667.5098
240.22580.1017-0.04320.50910.22790.15320.0552-0.4999-0.63390.30.5188-0.46060.1296-0.39060.10071.3719-0.4786-0.46381.04520.40520.855544.0045-25.376293.0254
250.1039-0.0802-0.0156-0.00790.02560.04920.0996-0.03410.17410.11580.0358-0.30780.1738-0.188600.7052-0.0607-0.1480.52640.02580.660739.9426-15.230974.8762
260.688-0.2334-0.01850.152-0.07640.13060.4720.4666-0.3596-0.2468-0.235-0.71310.5199-0.0396-0.0090.6869-0.026-0.18750.40790.00180.627234.9117-19.601350.4553
270.42050.1017-0.27010.11110.1060.62130.05770.09140.40611.017-0.1032-0.33910.79390.1772-0.04411.02830.0081-0.23540.4383-0.14780.873836.4201-23.481467.4221
280.1289-0.1531-0.2020.23250.50681.43050.17130.25710.6143-0.34840.29470.33250.31630.49880.02010.9774-0.019-0.39450.53570.06560.956242.1556-23.503659.7764
291.82010.5196-0.45070.4576-0.32720.22770.27360.3864-0.39040.27860.2879-0.35610.46880.05680.76590.8107-0.177-0.33470.55310.03680.808328.8214-20.541151.435
300.07520.2071-0.03130.2362-0.3530.17110.25370.36220.0762-0.274-0.02280.30080.3689-0.034-00.64980.05140.03490.7706-0.00620.510418.6858-10.397721.7554
310.2987-0.1238-0.21840.01840.00730.1494-0.16060.07830.04-0.4468-0.37920.57-0.23650.4204-0.00020.908-0.0706-0.25250.5571-0.07830.807919.703-22.979618.935
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 11 through 114 )
2X-RAY DIFFRACTION2chain 'A' and (resid 115 through 256 )
3X-RAY DIFFRACTION3chain 'A' and (resid 257 through 320 )
4X-RAY DIFFRACTION4chain 'B' and (resid 11 through 51 )
5X-RAY DIFFRACTION5chain 'B' and (resid 52 through 66 )
6X-RAY DIFFRACTION6chain 'B' and (resid 67 through 114 )
7X-RAY DIFFRACTION7chain 'B' and (resid 115 through 162 )
8X-RAY DIFFRACTION8chain 'B' and (resid 163 through 182 )
9X-RAY DIFFRACTION9chain 'B' and (resid 183 through 204 )
10X-RAY DIFFRACTION10chain 'B' and (resid 205 through 287 )
11X-RAY DIFFRACTION11chain 'B' and (resid 288 through 320 )
12X-RAY DIFFRACTION12chain 'C' and (resid 11 through 51 )
13X-RAY DIFFRACTION13chain 'C' and (resid 52 through 66 )
14X-RAY DIFFRACTION14chain 'C' and (resid 67 through 114 )
15X-RAY DIFFRACTION15chain 'C' and (resid 115 through 162 )
16X-RAY DIFFRACTION16chain 'C' and (resid 163 through 182 )
17X-RAY DIFFRACTION17chain 'C' and (resid 183 through 204 )
18X-RAY DIFFRACTION18chain 'C' and (resid 205 through 287 )
19X-RAY DIFFRACTION19chain 'C' and (resid 288 through 320 )
20X-RAY DIFFRACTION20chain 'D' and (resid 11 through 114 )
21X-RAY DIFFRACTION21chain 'D' and (resid 115 through 256 )
22X-RAY DIFFRACTION22chain 'D' and (resid 257 through 320 )
23X-RAY DIFFRACTION23chain 'E' and (resid 11 through 51 )
24X-RAY DIFFRACTION24chain 'E' and (resid 52 through 66 )
25X-RAY DIFFRACTION25chain 'E' and (resid 67 through 114 )
26X-RAY DIFFRACTION26chain 'E' and (resid 115 through 136 )
27X-RAY DIFFRACTION27chain 'E' and (resid 137 through 162 )
28X-RAY DIFFRACTION28chain 'E' and (resid 163 through 182 )
29X-RAY DIFFRACTION29chain 'E' and (resid 183 through 204 )
30X-RAY DIFFRACTION30chain 'E' and (resid 205 through 287 )
31X-RAY DIFFRACTION31chain 'E' and (resid 288 through 320 )

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