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- PDB-5tw7: Crystal structure of a GMP synthase (glutamine-hydrolyzing) from ... -

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Basic information

Entry
Database: PDB / ID: 5tw7
TitleCrystal structure of a GMP synthase (glutamine-hydrolyzing) from Neisseria gonorrhoeae
ComponentsGMP synthase [glutamine-hydrolyzing]
KeywordsLIGASE / Neisseria gonorrhoeae / GMP / glutamine / structural genomics / NIAID / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


GMP synthase (glutamine-hydrolyzing) activity / GMP synthase (glutamine-hydrolysing) / pyrophosphatase activity / glutamine metabolic process / ATP binding
Similarity search - Function
GMP synthase / GMP synthase, C-terminal / GMP synthetase ATP pyrophosphatase domain / GMP synthase C terminal domain / GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile. / GMP synthase, glutamine amidotransferase / GMP Synthetase; Chain A, domain 3 - #10 / NAD/GMP synthase / NAD synthase / Glutamine amidotransferase class-I ...GMP synthase / GMP synthase, C-terminal / GMP synthetase ATP pyrophosphatase domain / GMP synthase C terminal domain / GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile. / GMP synthase, glutamine amidotransferase / GMP Synthetase; Chain A, domain 3 - #10 / NAD/GMP synthase / NAD synthase / Glutamine amidotransferase class-I / Glutamine amidotransferase / Glutamine amidotransferase type 1 domain profile. / Class I glutamine amidotransferase (GATase) domain / GMP Synthetase; Chain A, domain 3 / Class I glutamine amidotransferase-like / HUPs / Rossmann-like alpha/beta/alpha sandwich fold / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GMP synthase [glutamine-hydrolyzing]
Similarity search - Component
Biological speciesNeisseria gonorrhoeae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.35 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To be Published
Title: Crystal structure of a GMP synthase (glutamine-hydrolyzing) from Neisseria gonorrhoeae
Authors: Edwards, T.E. / Abendroth, J. / Lorimer, D. / Fairman, J.W. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
History
DepositionNov 11, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 23, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Refinement description / Category: software
Revision 1.2Oct 4, 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 / pdbx_struct_conn_angle / struct_conn
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GMP synthase [glutamine-hydrolyzing]
B: GMP synthase [glutamine-hydrolyzing]
C: GMP synthase [glutamine-hydrolyzing]
D: GMP synthase [glutamine-hydrolyzing]
E: GMP synthase [glutamine-hydrolyzing]
F: GMP synthase [glutamine-hydrolyzing]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)352,5918
Polymers352,5436
Non-polymers492
Water6,053336
1
A: GMP synthase [glutamine-hydrolyzing]
D: GMP synthase [glutamine-hydrolyzing]


Theoretical massNumber of molelcules
Total (without water)117,5142
Polymers117,5142
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3330 Å2
ΔGint-17 kcal/mol
Surface area38530 Å2
MethodPISA
2
B: GMP synthase [glutamine-hydrolyzing]
E: GMP synthase [glutamine-hydrolyzing]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,5393
Polymers117,5142
Non-polymers241
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3430 Å2
ΔGint-24 kcal/mol
Surface area38550 Å2
MethodPISA
3
C: GMP synthase [glutamine-hydrolyzing]
F: GMP synthase [glutamine-hydrolyzing]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,5393
Polymers117,5142
Non-polymers241
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-25 kcal/mol
Surface area39380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)108.390, 109.350, 109.910
Angle α, β, γ (deg.)115.33, 100.00, 108.06
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
GMP synthase [glutamine-hydrolyzing] / GMP synthetase / Glutamine amidotransferase


Mass: 58757.113 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neisseria gonorrhoeae (bacteria) / Gene: guaA, NGK_2643 / Production host: Escherichia coli (E. coli)
References: UniProt: B4RJH7, GMP synthase (glutamine-hydrolysing)
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 336 / 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: 2.96 Å3/Da / Density % sol: 58.51 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: NegoA.17876.a.B1.PW39722 at 25.5 mg/mL against MCSG1 screen condition C6: 0.2 M magnesium chloride, 0.1 M HEPES, pH 7.5, 30% PEG400

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 20, 2016
RadiationMonochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.35→46.116 Å / Num. obs: 166001 / % possible obs: 98.1 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 34.37 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.075 / Rrim(I) all: 0.087 / Χ2: 0.998 / Net I/σ(I): 14.95 / Num. measured all: 644834
Reflection shell

Diffraction-ID: 1

Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2% possible all
2.35-2.410.5172.884849912497121930.80397.6
2.41-2.480.4413.390.84297.7
2.48-2.550.3694.040.89697.8
2.55-2.630.3094.850.92397.9
2.63-2.710.2525.950.94397.8
2.71-2.810.2087.130.95798.2
2.81-2.910.178.530.97198.2
2.91-3.030.13110.840.98298.2
3.03-3.170.10413.240.98898.3
3.17-3.320.07916.480.99398.4
3.32-3.50.06319.910.99598.2
3.5-3.720.05322.930.99698.4
3.72-3.970.04426.40.99798.4
3.97-4.290.03829.790.99798.2
4.29-4.70.03432.330.99898
4.7-5.250.03432.80.99798.3
5.25-6.070.03631.050.99898.3
6.07-7.430.03332.970.99898.7
7.43-10.510.02639.450.99897.9
10.51-46.1160.02641.020.99895.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XSCALEdata scaling
MOLREPphasing
PDB_EXTRACT3.2data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1GPM
Resolution: 2.35→46.116 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 23.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2232 7928 4.78 %
Rwork0.1858 --
obs0.1875 165962 98.33 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.35→46.116 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22619 0 2 336 22957
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00823182
X-RAY DIFFRACTIONf_angle_d0.89431504
X-RAY DIFFRACTIONf_dihedral_angle_d15.56213774
X-RAY DIFFRACTIONf_chiral_restr0.0563545
X-RAY DIFFRACTIONf_plane_restr0.0064123
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.35-2.37670.3132840.24935202X-RAY DIFFRACTION97
2.3767-2.40460.29592550.24085233X-RAY DIFFRACTION98
2.4046-2.4340.27632530.23335248X-RAY DIFFRACTION98
2.434-2.46480.27682730.23085279X-RAY DIFFRACTION98
2.4648-2.49720.27482840.2255240X-RAY DIFFRACTION98
2.4972-2.53140.26292660.21925202X-RAY DIFFRACTION98
2.5314-2.56760.29542760.22875231X-RAY DIFFRACTION98
2.5676-2.60590.29882810.22515248X-RAY DIFFRACTION98
2.6059-2.64660.26622760.22345254X-RAY DIFFRACTION98
2.6466-2.690.26812380.21975259X-RAY DIFFRACTION98
2.69-2.73640.26432720.21935261X-RAY DIFFRACTION98
2.7364-2.78610.27382480.22665292X-RAY DIFFRACTION98
2.7861-2.83970.31892530.22765289X-RAY DIFFRACTION98
2.8397-2.89770.26062830.22645232X-RAY DIFFRACTION98
2.8977-2.96070.26172480.22255317X-RAY DIFFRACTION98
2.9607-3.02950.26222640.21785267X-RAY DIFFRACTION99
3.0295-3.10530.3022510.22695283X-RAY DIFFRACTION98
3.1053-3.18920.25632800.2215275X-RAY DIFFRACTION98
3.1892-3.2830.24012700.21715283X-RAY DIFFRACTION99
3.283-3.38890.2472860.19955238X-RAY DIFFRACTION99
3.3889-3.510.2432620.19055309X-RAY DIFFRACTION99
3.51-3.65050.21332580.1795307X-RAY DIFFRACTION99
3.6505-3.81660.20082580.16895274X-RAY DIFFRACTION99
3.8166-4.01770.1972510.15625312X-RAY DIFFRACTION99
4.0177-4.26920.17932150.14795300X-RAY DIFFRACTION98
4.2692-4.59860.16642750.13315262X-RAY DIFFRACTION98
4.5986-5.06090.15032660.13545285X-RAY DIFFRACTION99
5.0609-5.7920.1922830.15845302X-RAY DIFFRACTION99
5.792-7.29260.19752410.16695330X-RAY DIFFRACTION99
7.2926-46.12460.15842780.1565220X-RAY DIFFRACTION98
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)
13.83980.3474-0.20582.3337-0.38811.5777-0.003-0.0491-0.0916-0.0927-0.00510.0138-0.02160.05960.02820.2077-0.06040.01280.4376-0.06790.2412-75.828712.342958.0307
22.716-0.4721-0.21542.8809-1.36882.8432-0.1016-0.2910.23080.3094-0.121-0.2912-0.19420.3990.18220.2302-0.0366-0.05120.3059-0.02830.2907-63.5133-21.857220.9554
30.6120.568-0.46621.43880.03770.5731-0.07680.41480.93160.0860.32680.5588-0.1157-0.2082-0.20230.32930.0742-0.07090.44140.19080.8632-62.78818.9589-0.4866
43.2465-0.07860.51712.2995-0.01643.41750.00430.31690.1202-0.04630.04540.205-0.1397-0.143-0.04560.17020.0001-0.03460.25410.02470.4734-37.18775.51351.4155
53.21921.17541.33393.9665-0.07784.2574-0.1734-0.2407-0.67180.11550.08960.04270.4019-0.09440.05830.28040.04970.13040.33020.03650.4794-101.069143.34225.9307
61.86240.0770.15480.73090.39484.7147-0.2138-0.0344-0.5006-0.09390.00540.02790.19940.12870.23240.2646-0.00820.08390.324-0.00090.4403-94.338549.39260.9553
71.3689-0.37160.5590.68550.00931.163-0.1317-0.9162-0.28950.1710.17620.09220.0928-0.53130.01010.40810.06920.11350.80550.21640.448-89.484949.065636.3379
84.235-0.374-0.10192.2830.53372.91820.0323-0.2780.2720.16860.12190.1603-0.0444-0.2891-0.13810.21410.03980.04440.33660.09320.3476-66.503751.981528.7899
92.1615-0.12080.02713.96711.121.81890.03650.62160.1934-0.3873-0.134-0.0002-0.1465-0.08420.0740.2659-0.0166-0.0130.52970.03580.2461-117.951727.727971.9553
100.45290.46460.45911.01260.79711.292-0.0560.6548-0.50350.0705-0.20470.39420.0794-0.56130.37360.3542-0.42410.12571.0095-0.68330.7733-123.5878-5.704862.8617
110.86830.0571-0.75710.83480.60632.3397-0.31410.5043-0.597-0.014-0.31640.22830.1414-0.67650.31480.4-0.16260.09180.6826-0.35540.4778-110.1196-6.066955.1017
122.93380.7360.28072.98870.2852.8417-0.0550.0019-0.26440.0122-0.1159-0.02370.1279-0.13130.14530.2017-0.08050.02940.4245-0.04930.2964-87.61841.630659.3408
130.88550.12550.12351.22391.51413.4153-0.12950.17170.345-0.1704-0.0520.0549-0.2448-0.00270.14440.25220.0212-0.050.23430.06690.32286.235-6.5747-12.7358
142.0363-1.4961-0.80261.61680.24840.80550.0396-0.19450.32040.02440.1585-0.1372-0.06880.1374-0.17340.2936-0.0138-0.05480.1803-0.0650.3977-0.254610.203116.7804
151.66320.11660.41782.17750.72342.74610.0713-0.0482-0.31530.14370.0110.05030.0137-0.0472-0.09140.19160.0151-0.01620.16950.03860.4488-23.57263.546412.2398
162.2153-0.28870.12463.23020.83661.9652-0.0543-0.15810.07210.1214-0.03920.21120.0873-0.03580.0970.2301-0.00260.01570.1142-0.01180.206-26.891378.701121.7354
171.67610.3476-0.27981.4362-0.38281.2872-0.0244-0.1377-0.09080.08550.0237-0.1969-0.0614-0.1097-0.00370.25840.0366-0.02520.16330.03190.2148-30.491740.610320.6224
183.3994-0.57850.18023.430.95373.66050.03180.00850.20660.07320.06460.16690.0794-0.0821-0.10250.14770.01190.00940.27570.08950.2345-54.141647.520520.0043
192.2491-0.0428-0.21382.282-1.27083.6043-0.02250.2936-0.2606-0.36760.051-0.04980.45730.0227-0.03730.3397-0.0001-0.00490.2079-0.01230.184-44.3659-1.240780.6153
202.40750.33620.04210.8628-0.19011.8612-0.12690.50620.0712-0.05-0.07970.01090.24280.16830.19170.3266-0.0330.03120.46070.04880.1777-53.431617.838548.8736
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'C' and (resid 428 through 521 )
2X-RAY DIFFRACTION2chain 'D' and (resid 2 through 199 )
3X-RAY DIFFRACTION3chain 'D' and (resid 200 through 396 )
4X-RAY DIFFRACTION4chain 'D' and (resid 397 through 521 )
5X-RAY DIFFRACTION5chain 'E' and (resid 3 through 75 )
6X-RAY DIFFRACTION6chain 'E' and (resid 76 through 227 )
7X-RAY DIFFRACTION7chain 'E' and (resid 228 through 396 )
8X-RAY DIFFRACTION8chain 'E' and (resid 397 through 521 )
9X-RAY DIFFRACTION9chain 'F' and (resid 1 through 199 )
10X-RAY DIFFRACTION10chain 'F' and (resid 200 through 227 )
11X-RAY DIFFRACTION11chain 'F' and (resid 228 through 396 )
12X-RAY DIFFRACTION12chain 'F' and (resid 397 through 521 )
13X-RAY DIFFRACTION13chain 'A' and (resid 3 through 227 )
14X-RAY DIFFRACTION14chain 'A' and (resid 228 through 396 )
15X-RAY DIFFRACTION15chain 'A' and (resid 397 through 521 )
16X-RAY DIFFRACTION16chain 'B' and (resid 2 through 199 )
17X-RAY DIFFRACTION17chain 'B' and (resid 200 through 427 )
18X-RAY DIFFRACTION18chain 'B' and (resid 428 through 521 )
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 199 )
20X-RAY DIFFRACTION20chain 'C' and (resid 200 through 427 )

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