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- PDB-4kzt: Structure mmNAGS bound with L-arginine -

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Basic information

Entry
Database: PDB / ID: 4kzt
TitleStructure mmNAGS bound with L-arginine
ComponentsN-acetylglutamate kinase / N-acetylglutamate synthase
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / synthetase / kinase / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


acetylglutamate kinase / acetylglutamate kinase activity / arginine biosynthetic process / acyltransferase activity, transferring groups other than amino-acyl groups / phosphorylation / cytoplasm
Similarity search - Function
Acetylglutamate kinase ArgB, GNAT domain-containing / N-Acetyl-L-glutamate kinase, fungal-type / Vertebrate-like NAGS Gcn5-related N-acetyltransferase (GNAT) domain / NAT, N-acetyltransferase, of N-acetylglutamate synthase / Vertebrate-like NAGS Gcn5-related N-acetyltransferase (GNAT) domain profile. / Acetylglutamate kinase family / Carbamate kinase / Acetylglutamate kinase-like / Aspartate/glutamate/uridylate kinase / Amino acid kinase family ...Acetylglutamate kinase ArgB, GNAT domain-containing / N-Acetyl-L-glutamate kinase, fungal-type / Vertebrate-like NAGS Gcn5-related N-acetyltransferase (GNAT) domain / NAT, N-acetyltransferase, of N-acetylglutamate synthase / Vertebrate-like NAGS Gcn5-related N-acetyltransferase (GNAT) domain profile. / Acetylglutamate kinase family / Carbamate kinase / Acetylglutamate kinase-like / Aspartate/glutamate/uridylate kinase / Amino acid kinase family / Acetylglutamate kinase-like superfamily / Gcn5-related N-acetyltransferase (GNAT) / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Aminopeptidase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ARGININE / DI(HYDROXYETHYL)ETHER / Acetylglutamate kinase
Similarity search - Component
Biological speciesMaricaulis maris (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.8 Å
AuthorsZhao, G. / Jin, Z. / Allewell, N.M. / Tuchman, M. / Shi, D.
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2013
Title: Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound.
Authors: Zhao, G. / Haskins, N. / Jin, Z. / M Allewell, N. / Tuchman, M. / Shi, D.
History
DepositionMay 30, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 16, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Revision 1.2Sep 20, 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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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: N-acetylglutamate kinase / N-acetylglutamate synthase
B: N-acetylglutamate kinase / N-acetylglutamate synthase
X: N-acetylglutamate kinase / N-acetylglutamate synthase
Y: N-acetylglutamate kinase / N-acetylglutamate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)202,05612
Polymers200,9314
Non-polymers1,1258
Water32418
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12580 Å2
ΔGint-0 kcal/mol
Surface area70650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)165.829, 110.823, 117.196
Angle α, β, γ (deg.)90.000, 91.020, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
N-acetylglutamate kinase / N-acetylglutamate synthase


Mass: 50232.758 Da / Num. of mol.: 4 / Mutation: I106M, I294M, L376M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Maricaulis maris (bacteria) / Strain: MCS10 / Gene: argA/B, Mmar10_0365 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q0ASS9, amino-acid N-acetyltransferase, acetylglutamate kinase
#2: Chemical
ChemComp-ARG / ARGININE / Arginine


Type: L-peptide linking / Mass: 175.209 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H15N4O2
#3: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 18 / 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: 2.68 Å3/Da / Density % sol: 54.09 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.2
Details: 100 mM cacodylic acid sodium salt trihydrate, pH 6.2, 25% polypropylene glycol P400 and 200 mM magnesium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 26, 2011
RadiationMonochromator: Si 111 xgannel / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionRedundancy: 6.6 % / Av σ(I) over netI: 36.98 / Number: 312380 / Rmerge(I) obs: 0.081 / Χ2: 2.37 / D res high: 2.8 Å / D res low: 50 Å / Num. obs: 47676 / % possible obs: 90.3
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
7.595096.910.0483.6996.4
6.037.5999.910.0563.4587.1
5.276.0310010.0643.3367.2
4.795.2799.910.0653.4797.1
4.444.7910010.0713.3857.2
4.184.4410010.083.0477.4
3.974.1810010.0992.8287.5
3.83.9710010.1232.4667.6
3.653.810010.1452.1987.6
3.533.6510010.1681.9617.6
3.423.5399.910.2061.6947.4
3.323.4299.910.251.4837.1
3.233.3298.710.2841.3916.6
3.153.2394.610.3411.266.1
3.083.1586.810.4061.2455.8
3.023.087910.4691.2165.4
2.963.0272.510.4861.1624.7
2.92.9664.210.5961.2134.1
2.852.957.810.581.163.5
2.82.8554.110.6561.1372.9
ReflectionResolution: 2.8→50 Å / Num. all: 52797 / Num. obs: 47676 / % possible obs: 90.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Rmerge(I) obs: 0.081 / Χ2: 2.365 / Net I/σ(I): 13.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.8-2.852.90.65614311.137154.1
2.85-2.93.50.5814901.16157.8
2.9-2.964.10.59617071.213164.2
2.96-3.024.70.48619131.162172.5
3.02-3.085.40.46920521.216179
3.08-3.155.80.40622881.245186.8
3.15-3.236.10.34125041.26194.6
3.23-3.326.60.28425791.391198.7
3.32-3.427.10.2526171.483199.9
3.42-3.537.40.20626391.694199.9
3.53-3.657.60.16826441.9611100
3.65-3.87.60.14526192.1981100
3.8-3.977.60.12326462.4661100
3.97-4.187.50.09926492.8281100
4.18-4.447.40.0826303.0471100
4.44-4.797.20.07126643.3851100
4.79-5.277.10.06526363.479199.9
5.27-6.037.20.06426523.3361100
6.03-7.597.10.05626723.458199.9
7.59-506.40.04826443.699196.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.11data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3S6H
Resolution: 2.8→39.298 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.7188 / SU ML: 0.43 / Cross valid method: THROUGHOUT / σ(F): 1.34 / σ(I): 0 / Phase error: 33.93 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2654 1998 4.2 %RANDOM
Rwork0.1957 ---
all0.1987 53056 --
obs0.1986 47618 89.75 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 242.21 Å2 / Biso mean: 102.4575 Å2 / Biso min: 33.08 Å2
Refinement stepCycle: LAST / Resolution: 2.8→39.298 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13244 0 76 18 13338
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00913544
X-RAY DIFFRACTIONf_angle_d1.35418376
X-RAY DIFFRACTIONf_chiral_restr0.0862096
X-RAY DIFFRACTIONf_plane_restr0.0072428
X-RAY DIFFRACTIONf_dihedral_angle_d15.2664976
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.8-2.85680.4829810.37841869195052
2.8568-2.9340.40571020.32652208231061
2.934-3.02030.39121190.27812584270372
3.0203-3.11780.32291290.2682966309582
3.1178-3.22920.33261440.25993375351993
3.2292-3.35840.34261560.25263590374699
3.3584-3.51120.29441540.232835903744100
3.5112-3.69610.28021600.205236423802100
3.6961-3.92750.28271570.19136043761100
3.9275-4.23040.23471610.177536243785100
4.2304-4.65560.23011560.156536433799100
4.6556-5.32780.23061600.164936403800100
5.3278-6.70710.291620.214236563818100
6.7071-39.2980.22581570.17053629378697
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)
14.84572.5171-3.09553.7952.10757.5295-0.03630.06171.42960.48080.4557-0.892-2.32761.8042-0.61011.8137-0.1966-0.45360.8691-0.04161.045128.6555139.9926-20.7427
26.8371.0101-0.69763.7623-1.01953.03520.0685-0.10410.1064-0.03320.16080.53560.0296-0.7235-0.28031.01380.0621-0.15130.62630.09760.631498.8491143.9327-21.1451
37.63081.7919-1.59756.6148-2.70157.2868-0.0471-0.9845-0.18191.367-0.12490.4304-0.2569-0.37080.07171.34330.0945-0.15770.59430.03910.54110.6284129.3943-9.0332
47.69190.65022.99324.68350.12145.37150.12250.4461-0.78580.99840.1441-0.10841.59410.5474-0.24371.740.2119-0.10570.54070.01560.6904128.9505112.5995-5.8343
53.627-1.49113.97465.4303-1.90615.11620.6038-0.098-0.53481.7826-0.2273-0.78210.52130.4442-0.32751.87780.0315-0.39210.68890.08290.6543136.3162121.09136.3837
66.24562.84632.53067.2584-2.7933.637-0.2656-1.68920.4003-0.2139-0.3969-2.15610.29542.42361.15190.74670.2186-0.12071.5202-0.05611.4787118.393175.8366-40.2115
77.31630.9474-0.59715.88790.13334.739-0.147-0.3494-0.7240.13740.17970.18691.2266-0.4211-0.01470.95940.0695-0.07040.62080.14080.566695.7774155.4677-40.3889
87.9861-2.15795.82825.5018-1.80138.53410.06550.54360.3266-0.1521-0.1775-0.18210.40850.54490.13340.42940.00650.00170.3968-0.00160.463897.8663173.9861-52.4991
92.17960.1621-1.71579.0179-0.79827.19930.32150.00690.69880.33560.12680.3167-0.3187-0.088-0.37890.5279-0.012-0.13830.5148-0.06071.1234103.4463198.1691-55.5329
108.15020.1662-4.79358.2659-1.72297.7490.50310.23671.6722-0.3374-0.1867-0.2901-0.19530.4797-0.23540.642-0.0623-0.1780.46680.03931.0658113.5011194.8056-68.3718
113.89944.394-0.51034.9634-0.59872.6594-0.35460.35881.24-0.9634-0.13562.39220.2026-0.80630.39061.4447-0.0178-0.28811.0536-0.25151.188128.1454155.2644-10.904
124.54930.1771-1.01313.215-1.52256.6608-0.04330.27820.15490.0412-0.592-0.8672-0.35521.27730.61231.45430.0781-0.35441.03030.09120.8044155.3912159.5446-23.6183
135.870.47890.48786.26870.10269.63260.3812-0.7509-0.65730.0979-0.6682-0.68640.32711.27180.23881.2168-0.034-0.23150.90860.08710.6348150.6439150.9354-3.6144
146.24841.4251.47226.23391.61996.05310.1568-0.74080.44261.4116-0.27530.2434-0.16350.27480.47421.83560.0518-0.30340.8502-0.15980.4893137.9285150.276118.2024
154.86550.8102-0.77793.3602-1.84715.62120.4768-0.5984-0.00171.2635-0.099-0.17470.727-0.1868-0.08171.8997-0.0717-0.28860.90060.0630.399132.9612134.530116.4195
161.85021.4989-1.65.3019-2.55146.00830.323-0.4724-0.12561.37740.79491.0582-0.2906-2.4148-0.94191.21820.24050.12281.45020.27411.1411125.2056163.7239-51.4651
177.50152.4529-0.984.5357-1.16056.62550.0525-0.51020.7910.4249-0.593-0.4827-1.01711.23890.63581.53120.1416-0.30030.99150.06920.7332151.3639174.0668-40.6593
186.48561.6745-1.67228.2161-1.4739.3725-0.55680.13481.07850.43470.2629-0.3042-1.31290.20670.11161.3940.2376-0.27010.63540.01810.6394142.1147178.2848-60.4399
196.4069-2.02-0.75777.13561.46564.3015-0.28820.2931-0.4497-0.72090.0455-0.33411.3301-0.1613-0.01861.5782-0.1241-0.09380.5006-0.04450.4586129.7468171.355-81.275
204.2245-2.0956-1.56868.9582.94139.14410.0990.5040.227-0.7160.17030.59840.2653-0.676-0.37880.9512-0.1179-0.18430.59360.09070.5139117.1535181.7988-78.8572
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 9:35)A9 - 35
2X-RAY DIFFRACTION2(chain A and resid 36:204)A36 - 204
3X-RAY DIFFRACTION3(chain A and resid 205:291)A205 - 291
4X-RAY DIFFRACTION4(chain A and resid 292:381)A292 - 381
5X-RAY DIFFRACTION5(chain A and resid 382:439)A382 - 439
6X-RAY DIFFRACTION6(chain B and resid 9:35)B9 - 35
7X-RAY DIFFRACTION7(chain B and resid 36:204)B36 - 204
8X-RAY DIFFRACTION8(chain B and resid 205:291)B205 - 291
9X-RAY DIFFRACTION9(chain B and resid 292:381)B292 - 381
10X-RAY DIFFRACTION10(chain B and resid 382:439)B382 - 439
11X-RAY DIFFRACTION11(chain X and resid 9:35)X9 - 35
12X-RAY DIFFRACTION12(chain X and resid 36:204)X36 - 204
13X-RAY DIFFRACTION13(chain X and resid 205:291)X205 - 291
14X-RAY DIFFRACTION14(chain X and resid 292:381)X292 - 381
15X-RAY DIFFRACTION15(chain X and resid 382:439)X382 - 439
16X-RAY DIFFRACTION16(chain Y and resid 9:35)Y9 - 35
17X-RAY DIFFRACTION17(chain Y and resid 36:204)Y36 - 204
18X-RAY DIFFRACTION18(chain Y and resid 205:291)Y205 - 291
19X-RAY DIFFRACTION19(chain Y and resid 292:381)Y292 - 381
20X-RAY DIFFRACTION20(chain Y and resid 382:439)Y382 - 439

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