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- PDB-2xmq: Crystal structure of human NDRG2 protein provides insight into it... -

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Basic information

Entry
Database: PDB / ID: 2xmq
TitleCrystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor
ComponentsPROTEIN NDRG2
KeywordsSIGNALING PROTEIN
Function / homology
Function and homology information


regulation of platelet-derived growth factor production / regulation of vascular endothelial growth factor production / vascular associated smooth muscle cell proliferation / negative regulation of cytokine production / negative regulation of vascular associated smooth muscle cell proliferation / substantia nigra development / negative regulation of ERK1 and ERK2 cascade / Wnt signaling pathway / growth cone / cell differentiation ...regulation of platelet-derived growth factor production / regulation of vascular endothelial growth factor production / vascular associated smooth muscle cell proliferation / negative regulation of cytokine production / negative regulation of vascular associated smooth muscle cell proliferation / substantia nigra development / negative regulation of ERK1 and ERK2 cascade / Wnt signaling pathway / growth cone / cell differentiation / perinuclear region of cytoplasm / Golgi apparatus / signal transduction / extracellular exosome / nucleus / cytosol / cytoplasm
Similarity search - Function
NDRG / Ndr family / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / Protein NDRG2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.81 Å
AuthorsHwang, J. / Kim, Y. / Lee, H. / Kim, M.H.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Crystal Structure of Human Ndrg2 Protein Provides Insight Into its Role as a Tumor Suppressor.
Authors: Hwang, J. / Kim, Y. / Kang, H.B. / Jaroszewski, L. / Deacon, A. / Lee, H. / Choi, W.C. / Kim, K.J. / Kim, C.H. / Kang, B.S. / Lee, J.O. / Oh, T.K. / Kim, J.W. / Wilson, I.A. / Kim, M.H.
History
DepositionJul 29, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 19, 2011Provider: repository / Type: Initial release
Revision 1.1Aug 31, 2011Group: Database references / Other / Version format compliance
Revision 1.2Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / 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 / _pdbx_database_status.status_code_sf / _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: PROTEIN NDRG2
B: PROTEIN NDRG2
C: PROTEIN NDRG2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,1936
Polymers94,0153
Non-polymers1773
Water1,67593
1
A: PROTEIN NDRG2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,3982
Polymers31,3381
Non-polymers591
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: PROTEIN NDRG2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,3982
Polymers31,3381
Non-polymers591
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: PROTEIN NDRG2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,3982
Polymers31,3381
Non-polymers591
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)86.411, 88.897, 126.799
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12B
22C
13C
23A

NCS domain segments:

Component-ID: 1 / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 1 / Auth seq-ID: 24 - 304 / Label seq-ID: 1 - 281

Dom-IDEns-IDAuth asym-IDLabel asym-ID
11AA
21BB
12BB
22CC
13CC
23AA

NCS ensembles :
ID
1
2
3

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Components

#1: Protein PROTEIN NDRG2 / NDRG2


Mass: 31338.482 Da / Num. of mol.: 3 / Fragment: ALPHA-BETA HYDROLASE DOMAIN, RESIDUES 24-304
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9UN36
#2: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 93 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.7 Å3/Da / Density % sol: 55 % / Description: NONE
Crystal growDetails: 9% PEG 8000, 0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE (PH 6.4 TO 7.5).

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 0.9795
DetectorDetector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.81→40 Å / Num. obs: 24361 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 6.6 % / Biso Wilson estimate: 0 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 19.1
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 4.5 / % possible all: 99

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2QMQ

2qmq


Resolution: 2.81→40 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.885 / SU B: 15.182 / SU ML: 0.297 / Cross valid method: THROUGHOUT / ESU R: 0 / ESU R Free: 0.4 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.25847 1242 5.1 %RANDOM
Rwork0.20095 ---
obs0.2039 23070 99.19 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 41.372 Å2
Baniso -1Baniso -2Baniso -3
1--0.11 Å20 Å20 Å2
2---1.11 Å20 Å2
3---1.22 Å2
Refinement stepCycle: LAST / Resolution: 2.81→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6615 0 12 93 6720
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0290.0226798
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.3321.9619255
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.4565840
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.24425318
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.222151083
X-RAY DIFFRACTIONr_dihedral_angle_4_deg25.8771524
X-RAY DIFFRACTIONr_chiral_restr0.1370.21005
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.025286
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.260.23047
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3380.24727
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1860.2227
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.3240.260
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3160.24
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1141.54290
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.83326807
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.37132820
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.5014.52448
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Number: 2205 / Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDTypeRms dev position (Å)Weight position
11Atight positional0.140.05
12Btight positional0.140.05
21Btight positional0.130.05
22Ctight positional0.130.05
31Ctight positional0.150.05
32Atight positional0.150.05
11Atight thermal0.180.5
12Btight thermal0.180.5
21Btight thermal0.210.5
22Ctight thermal0.210.5
31Ctight thermal0.190.5
32Atight thermal0.190.5
LS refinement shellResolution: 2.807→2.88 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.346 92 -
Rwork0.279 1572 -
obs--93.38 %

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