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- PDB-4q85: YcaO with Non-hydrolyzable ATP (AMPCPP) Bound -

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Basic information

Entry
Database: PDB / ID: 4q85
TitleYcaO with Non-hydrolyzable ATP (AMPCPP) Bound
ComponentsRibosomal protein S12 methylthiotransferase accessory factor YcaORibosome
KeywordsPROTEIN BINDING / YcaO ATP Binding Domain
Function / homology
Function and homology information


ATP diphosphatase activity / magnesium ion binding / cytosol
Similarity search - Function
YcaO cyclodehydratase, C-terminal / YcaO cyclodehydratase C-terminal domain / YcaO-like domain / YcaO cyclodehydratase, ATP-ad Mg2+-binding / YcaO domain profile.
Similarity search - Domain/homology
DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER / Ribosomal protein S12 methylthiotransferase accessory factor YcaO
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.29 Å
AuthorsChekan, J.R. / Nair, S.K.
CitationJournal: Nat.Chem.Biol. / Year: 2014
Title: Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.
Authors: Dunbar, K.L. / Chekan, J.R. / Cox, C.L. / Burkhart, B.J. / Nair, S.K. / Mitchell, D.A.
History
DepositionApr 25, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 13, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 3, 2014Group: Database references
Revision 1.2Oct 1, 2014Group: Database references
Revision 1.3Feb 28, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / software / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _software.name / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
B: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
C: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
D: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
E: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
F: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
G: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
H: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)528,60532
Polymers525,6178
Non-polymers2,98824
Water7,782432
1
A: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
B: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,56010
Polymers131,4042
Non-polymers1,1568
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5620 Å2
ΔGint-77 kcal/mol
Surface area44640 Å2
MethodPISA
2
C: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
D: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,0318
Polymers131,4042
Non-polymers6276
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4540 Å2
ΔGint-59 kcal/mol
Surface area45330 Å2
MethodPISA
3
E: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
F: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,9826
Polymers131,4042
Non-polymers5784
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4280 Å2
ΔGint-46 kcal/mol
Surface area46040 Å2
MethodPISA
4
G: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
H: Ribosomal protein S12 methylthiotransferase accessory factor YcaO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,0318
Polymers131,4042
Non-polymers6276
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4530 Å2
ΔGint-64 kcal/mol
Surface area45320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)110.282, 112.402, 130.683
Angle α, β, γ (deg.)89.40, 73.63, 77.62
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18B
28C
19B
29D
110B
210E
111B
211F
112B
212G
113B
213H
114C
214D
115C
215E
116C
216F
117C
217G
118C
218H
119D
219E
120D
220F
121D
221G
122D
222H
123E
223F
124E
224G
125E
225H
126F
226G
127F
227H
128G
228H

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALALYSLYSAA12 - 58012 - 580
21ALAALALYSLYSBB12 - 58012 - 580
12GLUGLUALAALAAA14 - 58114 - 581
22GLUGLUALAALACC14 - 58114 - 581
13ALAALALYSLYSAA12 - 58012 - 580
23ALAALALYSLYSDD12 - 58012 - 580
14ALAALALYSLYSAA12 - 58012 - 580
24ALAALALYSLYSEE12 - 58012 - 580
15ALAALALYSLYSAA12 - 58012 - 580
25ALAALALYSLYSFF12 - 58012 - 580
16SERSERLYSLYSAA25 - 58025 - 580
26SERSERLYSLYSGG25 - 58025 - 580
17ALAALALYSLYSAA12 - 58012 - 580
27ALAALALYSLYSHH12 - 58012 - 580
18GLUGLULYSLYSBB14 - 58014 - 580
28GLUGLULYSLYSCC14 - 58014 - 580
19THRTHRALAALABB2 - 5822 - 582
29THRTHRALAALADD2 - 5822 - 582
110THRTHRALAALABB2 - 5812 - 581
210THRTHRALAALAEE2 - 5812 - 581
111GLNGLNLYSLYSBB3 - 5803 - 580
211GLNGLNLYSLYSFF3 - 5803 - 580
112SERSERLYSLYSBB25 - 58025 - 580
212SERSERLYSLYSGG25 - 58025 - 580
113THRTHRTRPTRPBB2 - 5842 - 584
213THRTHRTRPTRPHH2 - 5842 - 584
114GLUGLULYSLYSCC14 - 58014 - 580
214GLUGLULYSLYSDD14 - 58014 - 580
115GLUGLULYSLYSCC14 - 58014 - 580
215GLUGLULYSLYSEE14 - 58014 - 580
116GLUGLULYSLYSCC14 - 58014 - 580
216GLUGLULYSLYSFF14 - 58014 - 580
117SERSERLYSLYSCC25 - 58025 - 580
217SERSERLYSLYSGG25 - 58025 - 580
118GLUGLULYSLYSCC14 - 58014 - 580
218GLUGLULYSLYSHH14 - 58014 - 580
119THRTHRALAALADD2 - 5812 - 581
219THRTHRALAALAEE2 - 5812 - 581
120GLNGLNLYSLYSDD3 - 5803 - 580
220GLNGLNLYSLYSFF3 - 5803 - 580
121SERSERLYSLYSDD25 - 58025 - 580
221SERSERLYSLYSGG25 - 58025 - 580
122THRTHRALAALADD2 - 5822 - 582
222THRTHRALAALAHH2 - 5822 - 582
123GLNGLNALAALAEE3 - 5813 - 581
223GLNGLNALAALAFF3 - 5813 - 581
124SERSERLYSLYSEE25 - 58025 - 580
224SERSERLYSLYSGG25 - 58025 - 580
125THRTHRALAALAEE2 - 5812 - 581
225THRTHRALAALAHH2 - 5812 - 581
126SERSERLYSLYSFF25 - 58025 - 580
226SERSERLYSLYSGG25 - 58025 - 580
127GLNGLNLYSLYSFF3 - 5803 - 580
227GLNGLNLYSLYSHH3 - 5803 - 580
128SERSERLYSLYSGG25 - 58025 - 580
228SERSERLYSLYSHH25 - 58025 - 580

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

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Components

#1: Protein
Ribosomal protein S12 methylthiotransferase accessory factor YcaO / Ribosome


Mass: 65702.109 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: ycaO, b0905, JW0888 / Production host: Escherichia coli (E. coli) / References: UniProt: P75838
#2: Chemical
ChemComp-APC / DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER / ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Comment: AMP-CPP, energy-carrying molecule analogue*YM
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: Mg
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 432 / Source method: isolated from a natural source / Formula: H2O

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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: 2.88 Å3/Da / Density % sol: 57.35 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 20% PEG 8,000 0.1 M magnesium acetate 0.1 M sodium cacodylate pH 6.5 6 mg/mL protein , VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 2, 2013
RadiationMonochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 3.29→125.2 Å / Num. all: 89486 / Num. obs: 88591 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.176 / Net I/σ(I): 2.5
Reflection shellResolution: 3.29→3.3 Å / Redundancy: 2.5 % / Mean I/σ(I) obs: 2.1 / Rsym value: 0.593 / % possible all: 98.2

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.8.0049refinement
autoPROCdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.29→125.2 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.861 / SU B: 26.163 / SU ML: 0.415 / Cross valid method: THROUGHOUT / ESU R Free: 0.528 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23928 4442 5 %RANDOM
Rwork0.19002 ---
obs0.19248 84143 99.04 %-
all-84993 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 63.451 Å2
Baniso -1Baniso -2Baniso -3
1-0.8 Å21.38 Å2-0.03 Å2
2--0.4 Å2-1.79 Å2
3----0.17 Å2
Refinement stepCycle: LAST / Resolution: 3.29→125.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms35815 0 174 432 36421
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01936875
X-RAY DIFFRACTIONr_bond_other_d0.0080.0233389
X-RAY DIFFRACTIONr_angle_refined_deg1.5071.95550208
X-RAY DIFFRACTIONr_angle_other_deg1.441376850
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.91554511
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.29424.8041890
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.818155731
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.48215183
X-RAY DIFFRACTIONr_chiral_restr0.0830.25393
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02142564
X-RAY DIFFRACTIONr_gen_planes_other0.0060.028726
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_it4.8946.24418092
X-RAY DIFFRACTIONr_mcbond_other4.8936.24518091
X-RAY DIFFRACTIONr_mcangle_it7.7589.36722587
X-RAY DIFFRACTIONr_mcangle_other7.8249.40622588
X-RAY DIFFRACTIONr_scbond_it4.9496.57718783
X-RAY DIFFRACTIONr_scbond_other4.9946.60318784
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other8.0619.77227622
X-RAY DIFFRACTIONr_long_range_B_refined12.60550.71342832
X-RAY DIFFRACTIONr_long_range_B_other12.60550.75242780
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)
11A337620.06
12B337620.06
21A333590.07
22C333590.07
31A336650.07
32D336650.07
41A339280.06
42E339280.06
51A324790.09
52F324790.09
61A321410.07
62G321410.07
71A338350.06
72H338350.06
81B333480.07
82C333480.07
91B346480.07
92D346480.07
101B344860.06
102E344860.06
111B325790.1
112F325790.1
121B321030.07
122G321030.07
131B349000.06
132H349000.06
141C332030.07
142D332030.07
151C338160.07
152E338160.07
161C319550.1
162F319550.1
171C319800.07
172G319800.07
181C334050.07
182H334050.07
191D342810.07
192E342810.07
201D324690.1
202F324690.1
211D319260.08
212G319260.08
221D343830.07
222H343830.07
231E328910.09
232F328910.09
241E321140.07
242G321140.07
251E343410.07
252H343410.07
261F309920.1
262G309920.1
271F325630.1
272H325630.1
281G321980.07
282H321980.07
LS refinement shellResolution: 3.287→3.372 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.326 342 -
Rwork0.292 6161 -
obs--98.65 %

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