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- PDB-9kpg: Crystal structure of human CASTOR2-arginine -

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Basic information

Entry
Database: PDB / ID: 9kpg
TitleCrystal structure of human CASTOR2-arginine
ComponentsCytosolic arginine sensor for mTORC1 subunit 2
KeywordsSIGNALING PROTEIN / CASTOR2 / mTORC1 / CASTOR
Function / homology
Function and homology information


cellular response to L-arginine / Amino acids regulate mTORC1 / negative regulation of TORC1 signaling / identical protein binding / cytosol
Similarity search - Function
CASTOR family / CASTOR1, N-terminal / : / Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain / Cytosolic arginine sensor for mTORC1 subunit 1/2, ACT-like / : / CASTOR, ACT domain / ACT domain / ACT-like domain
Similarity search - Domain/homology
ARGININE / : / Cytosolic arginine sensor for mTORC1 subunit 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å
AuthorsLiu, C. / Ding, J. / Zhang, T.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32070766 China
National Natural Science Foundation of China (NSFC)32271247 China
CitationJournal: Mol.Cell / Year: 2026
Title: CASTOR1 and CASTOR2 respond to different arginine levels to regulate mTORC1 activity.
Authors: Liu, C. / Zhang, Y. / Wang, Y. / Wu, M. / Li, Y. / Wei, J. / Shi, J. / Wang, R. / Su, L. / Yang, T. / Li, J. / Xiao, J. / Ding, J. / Zhang, T.
History
DepositionNov 22, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Mar 25, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytosolic arginine sensor for mTORC1 subunit 2
C: Cytosolic arginine sensor for mTORC1 subunit 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,94111
Polymers74,3172
Non-polymers6249
Water13,493749
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2920 Å2
ΔGint-14 kcal/mol
Surface area28160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)74.338, 48.391, 94.336
Angle α, β, γ (deg.)90.00, 106.06, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Cytosolic arginine sensor for mTORC1 subunit 2 / Cellular arginine sensor for mTORC1 protein 2 / GATS-like protein 2


Mass: 37158.371 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CASTOR2, GATSL1, GATSL2 / Production host: Escherichia coli (E. coli) / References: UniProt: A6NHX0
#2: Chemical ChemComp-ARG / ARGININE


Type: L-peptide linking / Mass: 175.209 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H15N4O2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: K
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 749 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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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: 2.19 Å3/Da / Density % sol: 43.94 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.1 M HEPES, 0.1 M KCl, and 15% PEG5000 MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9793 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 15, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.85→45.33 Å / Num. obs: 55304 / % possible obs: 97.6 % / Redundancy: 4.9 % / CC1/2: 0.99 / Rmerge(I) obs: 0.113 / Net I/σ(I): 7.4
Reflection shellResolution: 1.85→1.89 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.629 / Mean I/σ(I) obs: 2.2 / Num. unique obs: 4569 / CC1/2: 0.854 / % possible all: 84

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Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5GS9
Resolution: 1.85→45.33 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.04 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2302 3859 3.7 %0
Rwork0.1852 ---
obs0.1869 53971 96.56 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.85→45.33 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4842 0 31 749 5622
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0075084
X-RAY DIFFRACTIONf_angle_d0.8516930
X-RAY DIFFRACTIONf_dihedral_angle_d13.4441826
X-RAY DIFFRACTIONf_chiral_restr0.056820
X-RAY DIFFRACTIONf_plane_restr0.006879
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.85-1.870.33441100.29442830X-RAY DIFFRACTION76
1.87-1.90.32581170.26923122X-RAY DIFFRACTION85
1.9-1.920.28391260.26143293X-RAY DIFFRACTION89
1.92-1.950.27091310.23773407X-RAY DIFFRACTION92
1.95-1.980.2711340.23653431X-RAY DIFFRACTION94
1.98-20.27021410.2283642X-RAY DIFFRACTION97
2-2.040.23661360.22813548X-RAY DIFFRACTION97
2.04-2.070.26551440.22113650X-RAY DIFFRACTION98
2.07-2.110.28441400.20983707X-RAY DIFFRACTION98
2.11-2.140.24871340.21353494X-RAY DIFFRACTION96
2.14-2.180.26061430.2093670X-RAY DIFFRACTION99
2.18-2.230.2311410.19043626X-RAY DIFFRACTION99
2.23-2.280.26081430.1993719X-RAY DIFFRACTION100
2.28-2.330.24881420.18753714X-RAY DIFFRACTION100
2.33-2.390.26351410.1933696X-RAY DIFFRACTION100
2.39-2.450.23171430.19733674X-RAY DIFFRACTION100
2.45-2.530.29391420.19963701X-RAY DIFFRACTION99
2.53-2.610.27081390.19533678X-RAY DIFFRACTION99
2.61-2.70.25871480.19143724X-RAY DIFFRACTION99
2.7-2.810.24151360.18873589X-RAY DIFFRACTION98
2.81-2.940.2461440.18323709X-RAY DIFFRACTION99
2.94-3.090.19531430.17523687X-RAY DIFFRACTION100
3.09-3.280.21331440.1653694X-RAY DIFFRACTION99
3.28-3.540.1821420.15043695X-RAY DIFFRACTION99
3.54-3.890.20331410.14383665X-RAY DIFFRACTION99
3.89-4.460.14651360.13843629X-RAY DIFFRACTION98
4.46-5.610.18321430.1513670X-RAY DIFFRACTION99
5.61-100.23921350.20233648X-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)
11.53870.0461.11031.0038-0.37543.9939-0.1210.18680.1449-0.1456-0.0136-0.0779-0.30360.24290.12580.1426-0.02510.00710.06590.01330.107825.918-2.62414.475
21.94761.87363.25171.9637-3.0640.80270.21890.2407-0.321-0.5213-0.3984-0.99280.43160.57250.20880.26010.1270.02070.23030.090.413533.99-23.2732.529
32.68570.10191.28761.75150.52373.2554-0.02030.0269-0.00120.06940.0188-0.37470.00290.3921-0.00390.0853-0.01060.0060.10940.01780.143433.083-5.98732.841
40.9480.0594-0.20840.65910.4792.6816-0.04510.05760.0375-0.0344-0.0356-0.04430.0443-0.13510.09010.11670.0082-0.00520.0740.01650.111215.59-8.10419.687
52.80960.8449-0.42820.4833-1.04523.2019-0.09940.4691-0.551-0.1622-0.0704-0.04240.7484-0.52860.14610.2329-0.06660.02130.1788-0.06670.174312.066-17.52718.792
62.47180.5559-0.93861.454-0.75862.678-0.0017-0.15070.13630.0848-0.0164-0.0196-0.2141-0.09150.01660.08490.0208-0.02750.0778-0.00920.071914.683-4.90736.054
72.00032.00081.99942.00052.00032.00030.0007-0.0232-0.03680.03470.2731-0.0886-0.3687-0.3145-0.20060.23380.02840.0087-0.0715-0.05160.085421.331.09530.445
81.84620.05161.41292.8091-0.52764.5337-0.0156-0.01510.06670.09090.02070.1282-0.1869-0.2187-0.00180.08910.02710.0110.1288-0.01820.081111.419-1.163-12.01
91.38890.61420.44280.8301-0.61611.49340.08230.1699-0.1992-0.4227-0.06260.02250.3594-0.1996-0.00910.19980.0431-0.00290.2128-0.04380.18487.894-9.86-31.549
101.601-1.53081.28043.996-1.7624.12820.1966-0.1745-0.0747-0.22420.16060.36880.4442-0.939-0.31640.1455-0.0251-0.02580.2980.01460.1861-0.717-1.744-31.248
113.5665-0.5098-0.03120.34270.56190.56380.13910.28540.2468-0.018-0.2571-0.06250.12310.29910.10990.16080.0340.02050.1309-0.06230.115719.917-6.031-28.629
122.2211-0.4747-0.31232.91920.283.1553-0.01070.0776-0.40690.0248-0.067-0.21880.7730.42710.06880.31020.07750.01790.2063-0.01020.167221.099-16.213-12.488
132.2345-0.6651-1.57060.40281.12772.48390.13750.1460.0934-0.1549-0.0804-0.0665-0.12490.0049-0.05760.14240.06830.01360.17170.00950.126123.228-6.091-33.901
1426.89892.00018.07411.999720.07290.3488-0.0392-0.04050.07320.1464-0.19320.3179-0.17430.09450.12480.03680.12130.01030.123616.3641.266-29.021
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 1:82 )A1 - 82
2X-RAY DIFFRACTION2( CHAIN A AND RESID 83:96 )A83 - 96
3X-RAY DIFFRACTION3( CHAIN A AND RESID 97:165 )A97 - 165
4X-RAY DIFFRACTION4( CHAIN A AND RESID 166:236 )A166 - 236
5X-RAY DIFFRACTION5( CHAIN A AND RESID 237:269 )A237 - 269
6X-RAY DIFFRACTION6( CHAIN A AND RESID 270:334 )A270 - 334
7X-RAY DIFFRACTION7( CHAIN A AND RESID 401:401 )A401
8X-RAY DIFFRACTION8( CHAIN C AND RESID 1:75 )C1 - 75
9X-RAY DIFFRACTION9( CHAIN C AND RESID 76:122 )C76 - 122
10X-RAY DIFFRACTION10( CHAIN C AND RESID 123:165 )C123 - 165
11X-RAY DIFFRACTION11( CHAIN C AND RESID 166:192 )C166 - 192
12X-RAY DIFFRACTION12( CHAIN C AND RESID 193:263 )C193 - 263
13X-RAY DIFFRACTION13( CHAIN C AND RESID 264:335 )C264 - 335
14X-RAY DIFFRACTION14( CHAIN C AND RESID 401:401 )C401

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