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- PDB-7ndv: X-ray structure of acetylcholine-binding protein (AChBP) in compl... -

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Basic information

Entry
Database: PDB / ID: 7ndv
TitleX-ray structure of acetylcholine-binding protein (AChBP) in complex with FL001888.
ComponentsAcetylcholine-binding protein
KeywordsCHOLINE-BINDING PROTEIN / Fragment based drug design / Acetylcholine-binding protein
Function / homology
Function and homology information


acetylcholine receptor activity / acetylcholine-gated monoatomic cation-selective channel activity / synaptic cleft / response to nicotine / neuron projection / synapse / membrane
Similarity search - Function
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 / Ig-like domain profile. / Immunoglobulin-like domain
Similarity search - Domain/homology
4-[4-(trifluoromethyl)phenoxy]piperidine / Acetylcholine-binding protein
Similarity search - Component
Biological speciesLymnaea stagnalis (great pond snail)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsCederfelt, D. / Boronat, P. / Dobritzsch, D. / Hennig, S. / Fitzgerald, E.A. / de Esch, I.J.P. / Danielson, U.H.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
Marie Sklodowska-Curie Actions, FragNET ITN675899European Union
CitationJournal: RSC Advances / Year: 2021
Title: Discovery of fragments inducing conformational effects in dynamic proteins using a second-harmonic generation biosensor
Authors: Fitzgerald, E.A. / Butko, M.T. / Boronat, P. / Cederfelt, D. / Abramsson, M. / Ludviksdottir, H. / van Muijlwijk-Koezen, J. / de Esch, I.J.P. / Dobritzsch, D. / Young, T. / Danielson, U.H.
History
DepositionFeb 2, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 7, 2021Provider: repository / Type: Initial release
Revision 1.1Jan 31, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Acetylcholine-binding protein
B: Acetylcholine-binding protein
C: Acetylcholine-binding protein
D: Acetylcholine-binding protein
E: Acetylcholine-binding protein
F: Acetylcholine-binding protein
G: Acetylcholine-binding protein
H: Acetylcholine-binding protein
I: Acetylcholine-binding protein
J: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)274,30128
Polymers270,60310
Non-polymers3,69718
Water20,0871115
1
A: Acetylcholine-binding protein
B: Acetylcholine-binding protein
C: Acetylcholine-binding protein
D: Acetylcholine-binding protein
E: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,04213
Polymers135,3025
Non-polymers1,7418
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14300 Å2
ΔGint-55 kcal/mol
Surface area43090 Å2
MethodPISA
2
F: Acetylcholine-binding protein
G: Acetylcholine-binding protein
H: Acetylcholine-binding protein
I: Acetylcholine-binding protein
J: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,25815
Polymers135,3025
Non-polymers1,95710
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14700 Å2
ΔGint-99 kcal/mol
Surface area44340 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.680, 121.270, 239.300
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28I
19A
29J
110B
210C
111B
211D
112B
212E
113B
213F
114B
214G
115B
215H
116B
216I
117B
217J
118C
218D
119C
219E
120C
220F
121C
221G
122C
222H
123C
223I
124C
224J
125D
225E
126D
226F
127D
227G
128D
228H
129D
229I
130D
230J
131E
231F
132E
232G
133E
233H
134E
234I
135E
235J
136F
236G
137F
237H
138F
238I
139F
239J
140G
240H
141G
241I
142G
242J
143H
243I
144H
244J
145I
245J

NCS domain segments:

Component-ID: 0 / Beg auth comp-ID: LEU / Beg label comp-ID: LEU / Refine code: 0

Dom-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSLYSAA20 - 22320 - 223
21LYSLYSBB20 - 22320 - 223
12GLYGLYAA20 - 22420 - 224
22GLYGLYCC20 - 22420 - 224
13GLYGLYAA20 - 22420 - 224
23GLYGLYDD20 - 22420 - 224
14LYSLYSAA20 - 22320 - 223
24LYSLYSEE20 - 22320 - 223
15LYSLYSAA20 - 22320 - 223
25LYSLYSFF20 - 22320 - 223
16LYSLYSAA20 - 22320 - 223
26LYSLYSGG20 - 22320 - 223
17LYSLYSAA20 - 22320 - 223
27LYSLYSHH20 - 22320 - 223
18GLYGLYAA20 - 22420 - 224
28GLYGLYII20 - 22420 - 224
19LYSLYSAA20 - 22220 - 222
29LYSLYSJJ20 - 22220 - 222
110LYSLYSBB20 - 22320 - 223
210LYSLYSCC20 - 22320 - 223
111LYSLYSBB20 - 22320 - 223
211LYSLYSDD20 - 22320 - 223
112LYSLYSBB20 - 22220 - 222
212LYSLYSEE20 - 22220 - 222
113LYSLYSBB20 - 22220 - 222
213LYSLYSFF20 - 22220 - 222
114ILEILEBB20 - 22820 - 228
214ILEILEGG20 - 22820 - 228
115ILEILEBB20 - 22820 - 228
215ILEILEHH20 - 22820 - 228
116LYSLYSBB20 - 22320 - 223
216LYSLYSII20 - 22320 - 223
117LYSLYSBB20 - 22220 - 222
217LYSLYSJJ20 - 22220 - 222
118GLYGLYCC20 - 22420 - 224
218GLYGLYDD20 - 22420 - 224
119LYSLYSCC20 - 22220 - 222
219LYSLYSEE20 - 22220 - 222
120LYSLYSCC20 - 22320 - 223
220LYSLYSFF20 - 22320 - 223
121LYSLYSCC20 - 22320 - 223
221LYSLYSGG20 - 22320 - 223
122LYSLYSCC20 - 22320 - 223
222LYSLYSHH20 - 22320 - 223
123GLYGLYCC20 - 22420 - 224
223GLYGLYII20 - 22420 - 224
124LYSLYSCC20 - 22320 - 223
224LYSLYSJJ20 - 22320 - 223
125LYSLYSDD20 - 22320 - 223
225LYSLYSEE20 - 22320 - 223
126LYSLYSDD20 - 22320 - 223
226LYSLYSFF20 - 22320 - 223
127LYSLYSDD20 - 22320 - 223
227LYSLYSGG20 - 22320 - 223
128LYSLYSDD20 - 22320 - 223
228LYSLYSHH20 - 22320 - 223
129GLYGLYDD20 - 22420 - 224
229GLYGLYII20 - 22420 - 224
130LYSLYSDD20 - 22320 - 223
230LYSLYSJJ20 - 22320 - 223
131LYSLYSEE20 - 22320 - 223
231LYSLYSFF20 - 22320 - 223
132LYSLYSEE20 - 22220 - 222
232LYSLYSGG20 - 22220 - 222
133LYSLYSEE20 - 22220 - 222
233LYSLYSHH20 - 22220 - 222
134LYSLYSEE20 - 22320 - 223
234LYSLYSII20 - 22320 - 223
135LYSLYSEE20 - 22320 - 223
235LYSLYSJJ20 - 22320 - 223
136LYSLYSFF20 - 22220 - 222
236LYSLYSGG20 - 22220 - 222
137LYSLYSFF20 - 22220 - 222
237LYSLYSHH20 - 22220 - 222
138LYSLYSFF20 - 22320 - 223
238LYSLYSII20 - 22320 - 223
139LYSLYSFF20 - 22320 - 223
239LYSLYSJJ20 - 22320 - 223
140ILEILEGG20 - 22820 - 228
240ILEILEHH20 - 22820 - 228
141LYSLYSGG20 - 22320 - 223
241LYSLYSII20 - 22320 - 223
142LYSLYSGG20 - 22220 - 222
242LYSLYSJJ20 - 22220 - 222
143LYSLYSHH20 - 22320 - 223
243LYSLYSII20 - 22320 - 223
144LYSLYSHH20 - 22220 - 222
244LYSLYSJJ20 - 22220 - 222
145LYSLYSII20 - 22320 - 223
245LYSLYSJJ20 - 22320 - 223

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45

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Components

#1: Protein
Acetylcholine-binding protein / ACh-binding protein / AchBP


Mass: 27060.320 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lymnaea stagnalis (great pond snail) / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P58154
#2: Chemical
ChemComp-U8Q / 4-[4-(trifluoromethyl)phenoxy]piperidine


Mass: 245.241 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C12H14F3NO / Feature type: SUBJECT OF INVESTIGATION
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: SO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1115 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.06 Å3/Da / Density % sol: 40.17 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: PEG3350 3% Ammonium sulphate 1.8M HEPES buffer 0.1M, pH 7.75

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 0.976238 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 4, 2020
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976238 Å / Relative weight: 1
ReflectionResolution: 1.7→50 Å / Num. obs: 244709 / % possible obs: 100 % / Redundancy: 13.67 % / CC1/2: 0.999 / Net I/σ(I): 14.05
Reflection shellResolution: 1.7→1.7 Å / Num. unique obs: 38136 / CC1/2: 0.413

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
PHASERphasing
XSCALEdata scaling
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1UW6
Resolution: 1.7→48.27 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.955 / SU B: 3.664 / SU ML: 0.109 / Cross valid method: THROUGHOUT / ESU R: 0.118 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23314 12236 5 %RANDOM
Rwork0.20503 ---
obs0.20644 232473 99.97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 39.309 Å2
Baniso -1Baniso -2Baniso -3
1-2.03 Å20 Å2-0 Å2
2---1.12 Å20 Å2
3----0.91 Å2
Refinement stepCycle: 1 / Resolution: 1.7→48.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16304 0 243 1118 17665
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.01317085
X-RAY DIFFRACTIONr_bond_other_d0.0010.01715355
X-RAY DIFFRACTIONr_angle_refined_deg1.6121.65123367
X-RAY DIFFRACTIONr_angle_other_deg1.3491.57935716
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.44152074
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.121.903951
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.937152805
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.15515140
X-RAY DIFFRACTIONr_chiral_restr0.0690.22325
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0218929
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023625
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.4893.8428197
X-RAY DIFFRACTIONr_mcbond_other3.4833.8418196
X-RAY DIFFRACTIONr_mcangle_it4.7845.73610229
X-RAY DIFFRACTIONr_mcangle_other4.7845.73710230
X-RAY DIFFRACTIONr_scbond_it4.7994.4838888
X-RAY DIFFRACTIONr_scbond_other4.794.4788873
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other7.1836.4813090
X-RAY DIFFRACTIONr_long_range_B_refined9.14645.38618420
X-RAY DIFFRACTIONr_long_range_B_other9.13845.07718164
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A62870.09
12B62870.09
21A63070.1
22C63070.1
31A62930.1
32D62930.1
41A62320.1
42E62320.1
51A62850.09
52F62850.09
61A62830.1
62G62830.1
71A62480.1
72H62480.1
81A63300.09
82I63300.09
91A61940.1
92J61940.1
101B61980.09
102C61980.09
111B62130.09
112D62130.09
121B61710.08
122E61710.08
131B61220.1
132F61220.1
141B62420.1
142G62420.1
151B62570.11
152H62570.11
161B62130.09
162I62130.09
171B61600.09
172J61600.09
181C61920.1
182D61920.1
191C61030.09
192E61030.09
201C61860.1
202F61860.1
211C62810.08
212G62810.08
221C62320.09
222H62320.09
231C62270.09
232I62270.09
241C61710.1
242J61710.1
251D63450.08
252E63450.08
261D61970.11
262F61970.11
271D62640.1
272G62640.1
281D62400.1
282H62400.1
291D64610.07
292I64610.07
301D63510.07
302J63510.07
311E61300.1
312F61300.1
321E61080.09
322G61080.09
331E61420.09
332H61420.09
341E63240.08
342I63240.08
351E63560.07
352J63560.07
361F62570.11
362G62570.11
371F62350.11
372H62350.11
381F62130.1
382I62130.1
391F61280.11
392J61280.11
401G64360.11
402H64360.11
411G63070.1
412I63070.1
421G62010.1
422J62010.1
431H63060.09
432I63060.09
441H61480.1
442J61480.1
451I63610.08
452J63610.08
LS refinement shellResolution: 1.7→1.744 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.376 896 -
Rwork0.393 17027 -
obs--99.87 %

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