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- PDB-4i52: scMenB im complex with 1-hydroxy-2-naphthoyl-CoA -

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Basic information

Entry
Database: PDB / ID: 4i52
TitlescMenB im complex with 1-hydroxy-2-naphthoyl-CoA
ComponentsNaphthoate synthase
KeywordsLYASE / crotonase / 1 / 4-dihydroxy-2-naphthoyl coenzyme A synthase
Function / homology
Function and homology information


1,4-dihydroxy-2-naphthoyl-CoA synthase / 1,4-dihydroxy-2-naphthoyl-CoA synthase activity / phylloquinone biosynthetic process / menaquinone biosynthetic process / cytosol
Similarity search - Function
1,4-Dihydroxy-2-naphthoyl-CoA synthase, MenB / Lyase 2-enoyl-coa Hydratase, Chain A, domain 2 / Lyase 2-enoyl-coa Hydratase; Chain A, domain 2 / Enoyl-CoA hydratase, C-terminal / Enoyl-CoA hydratase/isomerase, conserved site / Enoyl-CoA hydratase/isomerase signature. / Enoyl-CoA hydratase/isomerase / Enoyl-CoA hydratase/isomerase / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 ...1,4-Dihydroxy-2-naphthoyl-CoA synthase, MenB / Lyase 2-enoyl-coa Hydratase, Chain A, domain 2 / Lyase 2-enoyl-coa Hydratase; Chain A, domain 2 / Enoyl-CoA hydratase, C-terminal / Enoyl-CoA hydratase/isomerase, conserved site / Enoyl-CoA hydratase/isomerase signature. / Enoyl-CoA hydratase/isomerase / Enoyl-CoA hydratase/isomerase / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
1-hydroxy-2-naphthoyl-CoA / 1,4-dihydroxy-2-naphthoyl-CoA synthase
Similarity search - Component
Biological speciesSynechocystis sp. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsSong, H.G. / Sun, Y.R. / Li, J. / Li, Y. / Jiang, M. / Zhou, J.H. / Guo, Z.H.
CitationJournal: Plos One / Year: 2013
Title: Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily
Authors: Sun, Y. / Song, H. / Li, J. / Li, Y. / Jiang, M. / Zhou, J. / Guo, Z.
History
DepositionNov 28, 2012Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 8, 2013Provider: repository / Type: Initial release
Revision 1.1Jun 19, 2013Group: Database references
Revision 1.2Nov 8, 2023Group: 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_initial_refinement_model / 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 / _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: Naphthoate synthase
B: Naphthoate synthase
C: Naphthoate synthase
D: Naphthoate synthase
E: Naphthoate synthase
F: Naphthoate synthase
G: Naphthoate synthase
H: Naphthoate synthase
I: Naphthoate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)281,85027
Polymers273,0929
Non-polymers8,75818
Water10,503583
1
A: Naphthoate synthase
C: Naphthoate synthase
D: Naphthoate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,9509
Polymers91,0313
Non-polymers2,9196
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7520 Å2
ΔGint-36 kcal/mol
Surface area35490 Å2
MethodPISA
2
B: Naphthoate synthase
E: Naphthoate synthase
F: Naphthoate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,9509
Polymers91,0313
Non-polymers2,9196
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7610 Å2
ΔGint-36 kcal/mol
Surface area35480 Å2
MethodPISA
3
G: Naphthoate synthase
H: Naphthoate synthase
I: Naphthoate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,9509
Polymers91,0313
Non-polymers2,9196
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7760 Å2
ΔGint-34 kcal/mol
Surface area35710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)138.843, 138.843, 221.217
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221
Components on special symmetry positions
IDModelComponents
11D-462-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28I
19B
29C
110B
210D
111B
211E
112B
212F
113B
213G
114B
214H
115B
215I
116C
216D
117C
217E
118C
218F
119C
219G
120C
220H
121C
221I
122D
222E
123D
223F
124D
224G
125D
225H
126D
226I
127E
227F
128E
228G
129E
229H
130E
230I
131F
231G
132F
232H
133F
233I
134G
234H
135G
235I
136H
236I

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11METMETPROPROAA1 - 2751 - 275
21METMETPROPROBB1 - 2751 - 275
12ASPASPLEULEUAA2 - 2742 - 274
22ASPASPLEULEUCC2 - 2742 - 274
13METMETPROPROAA1 - 2751 - 275
23METMETPROPRODD1 - 2751 - 275
14ASPASPLEULEUAA2 - 2742 - 274
24ASPASPLEULEUEE2 - 2742 - 274
15ASPASPLEULEUAA2 - 2742 - 274
25ASPASPLEULEUFF2 - 2742 - 274
16METMETPROPROAA1 - 2751 - 275
26METMETPROPROGG1 - 2751 - 275
17METMETPROPROAA1 - 2751 - 275
27METMETPROPROHH1 - 2751 - 275
18METMETPROPROAA1 - 2751 - 275
28METMETPROPROII1 - 2751 - 275
19ASPASPLEULEUBB2 - 2742 - 274
29ASPASPLEULEUCC2 - 2742 - 274
110METMETPROPROBB1 - 2751 - 275
210METMETPROPRODD1 - 2751 - 275
111ASPASPLEULEUBB2 - 2742 - 274
211ASPASPLEULEUEE2 - 2742 - 274
112ASPASPLEULEUBB2 - 2742 - 274
212ASPASPLEULEUFF2 - 2742 - 274
113METMETPROPROBB1 - 2751 - 275
213METMETPROPROGG1 - 2751 - 275
114METMETPROPROBB1 - 2751 - 275
214METMETPROPROHH1 - 2751 - 275
115METMETPROPROBB1 - 2751 - 275
215METMETPROPROII1 - 2751 - 275
116ASPASPLEULEUCC2 - 2742 - 274
216ASPASPLEULEUDD2 - 2742 - 274
117ASPASPPROPROCC2 - 2752 - 275
217ASPASPPROPROEE2 - 2752 - 275
118ASPASPPROPROCC2 - 2752 - 275
218ASPASPPROPROFF2 - 2752 - 275
119ASPASPLEULEUCC2 - 2742 - 274
219ASPASPLEULEUGG2 - 2742 - 274
120ASPASPLEULEUCC2 - 2742 - 274
220ASPASPLEULEUHH2 - 2742 - 274
121ASPASPLEULEUCC2 - 2742 - 274
221ASPASPLEULEUII2 - 2742 - 274
122ASPASPLEULEUDD2 - 2742 - 274
222ASPASPLEULEUEE2 - 2742 - 274
123ASPASPLEULEUDD2 - 2742 - 274
223ASPASPLEULEUFF2 - 2742 - 274
124METMETPROPRODD1 - 2751 - 275
224METMETPROPROGG1 - 2751 - 275
125METMETPROPRODD1 - 2751 - 275
225METMETPROPROHH1 - 2751 - 275
126METMETPROPRODD1 - 2751 - 275
226METMETPROPROII1 - 2751 - 275
127ASPASPPROPROEE2 - 2752 - 275
227ASPASPPROPROFF2 - 2752 - 275
128ASPASPLEULEUEE2 - 2742 - 274
228ASPASPLEULEUGG2 - 2742 - 274
129ASPASPLEULEUEE2 - 2742 - 274
229ASPASPLEULEUHH2 - 2742 - 274
130ASPASPLEULEUEE2 - 2742 - 274
230ASPASPLEULEUII2 - 2742 - 274
131ASPASPLEULEUFF2 - 2742 - 274
231ASPASPLEULEUGG2 - 2742 - 274
132ASPASPLEULEUFF2 - 2742 - 274
232ASPASPLEULEUHH2 - 2742 - 274
133ASPASPLEULEUFF2 - 2742 - 274
233ASPASPLEULEUII2 - 2742 - 274
134METMETPROPROGG1 - 2751 - 275
234METMETPROPROHH1 - 2751 - 275
135METMETPROPROGG1 - 2751 - 275
235METMETPROPROII1 - 2751 - 275
136METMETPROPROHH1 - 2751 - 275
236METMETPROPROII1 - 2751 - 275

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

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Components

#1: Protein
Naphthoate synthase


Mass: 30343.508 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Synechocystis sp. (bacteria) / Strain: PCC 6803 / Kazusa
References: UniProt: P73495, 1,4-dihydroxy-2-naphthoyl-CoA synthase
#2: Chemical
ChemComp-1HA / 1-hydroxy-2-naphthoyl-CoA


Mass: 937.698 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C32H42N7O18P3S
#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 583 / 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: 2.25 Å3/Da / Density % sol: 45.43 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 5.7
Details: 0.15M ammonium acetate, 0.3M ammonium sulfate, 16% PEG3350, 100mM Bis-Tris buffer, 0.1M Proline(or 0.1M Taurine), pH 5.70, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 15, 2011
RadiationMonochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2.35→46.596 Å / Num. all: 97846 / Num. obs: 102666 / % possible obs: 99.73 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3
Reflection shellResolution: 2.35→46.596 Å

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.7.0032refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EML
Resolution: 2.35→46.596 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.905 / SU B: 8.258 / SU ML: 0.195 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / ESU R: 0.582 / ESU R Free: 0.277 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25556 5135 5 %RANDOM
Rwork0.22884 ---
obs0.23016 97582 99.73 %-
all-103005 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 43.148 Å2
Baniso -1Baniso -2Baniso -3
1-0.94 Å20.94 Å20 Å2
2--0.94 Å20 Å2
3----3.04 Å2
Refinement stepCycle: LAST / Resolution: 2.35→46.596 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18830 0 558 583 19971
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01919834
X-RAY DIFFRACTIONr_bond_other_d0.0040.0218413
X-RAY DIFFRACTIONr_angle_refined_deg1.2971.99226956
X-RAY DIFFRACTIONr_angle_other_deg1.06342207
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.97352463
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.00823.684855
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.157153056
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.43515128
X-RAY DIFFRACTIONr_chiral_restr0.0630.22837
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02122635
X-RAY DIFFRACTIONr_gen_planes_other0.0030.024626
Refine LS restraints NCS

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

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A153160.06
12B153160.06
21A150130.07
22C150130.07
31A153310.07
32D153310.07
41A151290.05
42E151290.05
51A152290.06
52F152290.06
61A153880.05
62G153880.05
71A153400.06
72H153400.06
81A151280.07
82I151280.07
91B155170.06
92C155170.06
101B156730.06
102D156730.06
111B156150.05
112E156150.05
121B156640.06
122F156640.06
131B159510.04
132G159510.04
141B159550.05
142H159550.05
151B157260.06
152I157260.06
161C153890.07
162D153890.07
171C155390.06
172E155390.06
181C155600.06
182F155600.06
191C154730.06
192G154730.06
201C155620.06
202H155620.06
211C154060.06
212I154060.06
221D155320.06
222E155320.06
231D156720.05
232F156720.05
241D157180.06
242G157180.06
251D157700.06
252H157700.06
261D156880.06
262I156880.06
271E156460.06
272F156460.06
281E155830.04
282G155830.04
291E157110.05
292H157110.05
301E155610.06
302I155610.06
311F156700.06
312G156700.06
321F157840.06
322H157840.06
331F157220.05
332I157220.05
341G158860.06
342H158860.06
351G157160.06
352I157160.06
361H159250.06
362I159250.06
LS refinement shellResolution: 2.35→2.412 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.295 346 -
Rwork0.269 7109 -
obs-97582 99.67 %

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