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- PDB-3s3k: Crystal structure of the catalytic domain of PTP10D from Drosophi... -

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Basic information

Entry
Database: PDB / ID: 3s3k
TitleCrystal structure of the catalytic domain of PTP10D from Drosophila melanogaster with a small molecular inhibitor para-NitroCatechol Sulphate
ComponentsTyrosine-protein phosphatase 10D
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Differentiation / Neurogenesis / Signal transduction / developmental Protein / Hydrolase / Protein Phosphatase / Protein Tyrosine Phosphatase / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


branching involved in open tracheal system development / open tracheal system development / negative regulation of fibroblast growth factor receptor signaling pathway / Neutrophil degranulation / transmembrane receptor protein tyrosine phosphatase activity / motor neuron axon guidance / response to stimulus / negative regulation of epidermal growth factor receptor signaling pathway / negative regulation of vascular endothelial growth factor receptor signaling pathway / long-term memory ...branching involved in open tracheal system development / open tracheal system development / negative regulation of fibroblast growth factor receptor signaling pathway / Neutrophil degranulation / transmembrane receptor protein tyrosine phosphatase activity / motor neuron axon guidance / response to stimulus / negative regulation of epidermal growth factor receptor signaling pathway / negative regulation of vascular endothelial growth factor receptor signaling pathway / long-term memory / protein dephosphorylation / protein-tyrosine-phosphatase / central nervous system development / protein tyrosine phosphatase activity / axon guidance / apical part of cell / axon / membrane
Similarity search - Function
PTPRJ, transmembrane domain / TM proximal of protein tyrosine phosphatase, receptor type J / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif ...PTPRJ, transmembrane domain / TM proximal of protein tyrosine phosphatase, receptor type J / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM / Tyrosine-protein phosphatase 10D
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsMadan, L.L. / Gopal, B.
CitationJournal: Biochemistry / Year: 2011
Title: Conformational basis for substrate recruitment in protein tyrosine phosphatase 10D
Authors: Madan, L.L. / Gopal, B.
History
DepositionMay 18, 2011Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Nov 2, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 3, 2013Group: Database references
Revision 1.2Nov 1, 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_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_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_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: Tyrosine-protein phosphatase 10D
B: Tyrosine-protein phosphatase 10D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,1263
Polymers71,8912
Non-polymers2351
Water46826
1
A: Tyrosine-protein phosphatase 10D


Theoretical massNumber of molelcules
Total (without water)35,9461
Polymers35,9461
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Tyrosine-protein phosphatase 10D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,1812
Polymers35,9461
Non-polymers2351
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)102.510, 102.510, 172.800
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: LYS / End label comp-ID: LYS / Refine code: 4 / Auth seq-ID: 21 - 305 / Label seq-ID: 21 - 305

Dom-IDAuth asym-IDLabel asym-ID
1AA
2BB

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Components

#1: Protein Tyrosine-protein phosphatase 10D / Receptor-linked protein-tyrosine phosphatase 10D / DPTP10D


Mass: 35945.633 Da / Num. of mol.: 2 / Fragment: UNP residues 1250-1533
Source method: isolated from a genetically manipulated source
Details: Central nervous system / Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG1817, Ptp10D / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P35992, protein-tyrosine-phosphatase
#2: Chemical ChemComp-CSN / N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM


Mass: 235.171 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H5NO7S
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 26 / 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: 3.65 Å3/Da / Density % sol: 66.26 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 15% PEG 2000, 120mM Citrate, 10% iso-Propanol, 10% n-Butanol, 10% 1,4-Butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 30, 2010 / Details: bent collimating mirror with toroid
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→45 Å / Num. obs: 17564 / % possible obs: 98.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -5 / Redundancy: 3.1 % / Biso Wilson estimate: 56.63 Å2 / Rmerge(I) obs: 0.164 / Net I/σ(I): 4.7
Reflection shellResolution: 3.2→3.37 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.426 / Mean I/σ(I) obs: 2.4 / Num. unique all: 7809 / % possible all: 99

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3S3E

3s3e


Resolution: 3.2→44.08 Å / Cor.coef. Fo:Fc: 0.806 / Cor.coef. Fo:Fc free: 0.728 / SU B: 46.825 / SU ML: 0.391 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / ESU R Free: 0.546 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.30858 880 5.1 %RANDOM
Rwork0.25286 ---
all0.2557 16355 --
obs0.2557 16355 96.22 %-
Solvent computationSolvent model: BABINET MODEL PARAMETERS FOR MASK CACLULATION
Displacement parametersBiso mean: 54.071 Å2
Baniso -1Baniso -2Baniso -3
1-0.08 Å20.04 Å20 Å2
2--0.08 Å20 Å2
3----0.12 Å2
Refinement stepCycle: LAST / Resolution: 3.2→44.08 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4663 0 15 26 4704
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0214815
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1941.9276539
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5545570
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.14922.791258
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.9915765
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.941548
X-RAY DIFFRACTIONr_chiral_restr0.0880.2680
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213806
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCSNumber: 2252 / Type: medium positional / Rms dev position: 0.57 Å / Weight position: 0.5
LS refinement shellResolution: 3.2→3.283 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.337 75 -
Rwork0.248 1211 -
obs--98.77 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.39940.5089-0.04931.4489-0.30295.15070.00720.15170.08010.02210.01140.04950.0554-0.1548-0.01860.00490.0018-0.01760.0282-0.01420.1077-34.920313.475422.5585
22.0866-0.4217-0.61411.40210.08823.57310.04150.2181-0.0877-0.23730.02940.04330.155-0.1174-0.07090.0537-0.0157-0.00830.04190.02090.095-9.737333.3075-2.4947
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A19 - 305
2X-RAY DIFFRACTION2B21 - 305

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