[English] 日本語
Yorodumi
- PDB-8xoy: The Crystal Structure of PTP1B from Biortus. -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8xoy
TitleThe Crystal Structure of PTP1B from Biortus.
ComponentsTyrosine-protein phosphatase non-receptor type 1
KeywordsHYDROLASE / Protein phosphatase
Function / homology
Function and homology information


PTK6 Down-Regulation / regulation of hepatocyte growth factor receptor signaling pathway / positive regulation of receptor catabolic process / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of IRE1-mediated unfolded protein response / negative regulation of PERK-mediated unfolded protein response / IRE1-mediated unfolded protein response / regulation of intracellular protein transport ...PTK6 Down-Regulation / regulation of hepatocyte growth factor receptor signaling pathway / positive regulation of receptor catabolic process / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of IRE1-mediated unfolded protein response / negative regulation of PERK-mediated unfolded protein response / IRE1-mediated unfolded protein response / regulation of intracellular protein transport / cytoplasmic side of endoplasmic reticulum membrane / sorting endosome / mitochondrial crista / platelet-derived growth factor receptor-beta signaling pathway / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / positive regulation of protein tyrosine kinase activity / non-membrane spanning protein tyrosine phosphatase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / cellular response to unfolded protein / regulation of signal transduction / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / Growth hormone receptor signaling / MECP2 regulates neuronal receptors and channels / negative regulation of MAP kinase activity / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / negative regulation of insulin receptor signaling pathway / Insulin receptor recycling / protein dephosphorylation / ephrin receptor binding / Integrin signaling / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / protein phosphatase 2A binding / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytosol / cytoplasm
Similarity search - Function
Protein-tyrosine phosphatase, non-receptor type-1/2 / : / 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 ...Protein-tyrosine phosphatase, non-receptor type-1/2 / : / 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
Similarity search - Domain/homology
Tyrosine-protein phosphatase non-receptor type 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å
AuthorsWang, F. / Cheng, W. / Lv, Z. / Meng, Q. / Li, J.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: The Crystal Structure of PTP1B from Biortus.
Authors: Wang, F. / Cheng, W. / Lv, Z. / Meng, Q. / Li, J.
History
DepositionJan 2, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 24, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tyrosine-protein phosphatase non-receptor type 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,10314
Polymers37,4071
Non-polymers69613
Water7,350408
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area120 Å2
ΔGint-10 kcal/mol
Surface area13520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)88.148, 88.148, 103.396
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121

-
Components

-
Protein , 1 types, 1 molecules A

#1: Protein Tyrosine-protein phosphatase non-receptor type 1 / Protein-tyrosine phosphatase 1B / PTP-1B


Mass: 37406.625 Da / Num. of mol.: 1 / Mutation: C215S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PTPN1, PTP1B / Production host: Escherichia coli (E. coli) / References: UniProt: P18031, protein-tyrosine-phosphatase

-
Non-polymers , 5 types, 421 molecules

#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 408 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.1 Å3/Da / Density % sol: 60.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.2M MgCl2, 0.1M Bis-Tris pH6.5, 25% PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL45XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 7, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.55→44.07 Å / Num. obs: 67746 / % possible obs: 99.9 % / Redundancy: 8.7 % / Rmerge(I) obs: 0.089 / Net I/σ(I): 15
Reflection shellResolution: 1.55→1.58 Å / Rmerge(I) obs: 1.013 / Num. unique obs: 3347

-
Processing

Software
NameVersionClassification
REFMAC5.8.0419refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.55→44.07 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.963 / SU B: 1.181 / SU ML: 0.042 / Cross valid method: FREE R-VALUE / ESU R: 0.06 / ESU R Free: 0.062
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.1841 3409 5.035 %
Rwork0.1591 64293 -
all0.16 --
obs-67702 99.876 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 18.053 Å2
Baniso -1Baniso -2Baniso -3
1-0.043 Å20.021 Å20 Å2
2--0.043 Å2-0 Å2
3----0.138 Å2
Refinement stepCycle: LAST / Resolution: 1.55→44.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2446 0 38 409 2893
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0122608
X-RAY DIFFRACTIONr_bond_other_d0.0010.0162458
X-RAY DIFFRACTIONr_angle_refined_deg1.4361.663522
X-RAY DIFFRACTIONr_angle_other_deg0.5061.5845708
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9365326
X-RAY DIFFRACTIONr_dihedral_angle_2_deg5.361517
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.80410491
X-RAY DIFFRACTIONr_dihedral_angle_6_deg16.07310130
X-RAY DIFFRACTIONr_chiral_restr0.0750.2375
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.023067
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02597
X-RAY DIFFRACTIONr_nbd_refined0.2220.2511
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1810.22264
X-RAY DIFFRACTIONr_nbtor_refined0.1810.21277
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0790.21328
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1860.2317
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0020.21
X-RAY DIFFRACTIONr_metal_ion_refined0.4750.24
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.140.26
X-RAY DIFFRACTIONr_nbd_other0.1430.231
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2250.227
X-RAY DIFFRACTIONr_mcbond_it1.6711.6951230
X-RAY DIFFRACTIONr_mcbond_other1.6631.6941230
X-RAY DIFFRACTIONr_mcangle_it2.6313.0331544
X-RAY DIFFRACTIONr_mcangle_other2.6353.0381545
X-RAY DIFFRACTIONr_scbond_it2.92.0991378
X-RAY DIFFRACTIONr_scbond_other2.8992.11379
X-RAY DIFFRACTIONr_scangle_it4.6733.6431965
X-RAY DIFFRACTIONr_scangle_other4.6723.6451966
X-RAY DIFFRACTIONr_lrange_it6.83322.1283166
X-RAY DIFFRACTIONr_lrange_other6.54817.1283000
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.55-1.590.272490.2724691X-RAY DIFFRACTION99.9595
1.59-1.6340.2552400.2484606X-RAY DIFFRACTION100
1.634-1.6810.2722030.2294474X-RAY DIFFRACTION100
1.681-1.7330.2162440.2064334X-RAY DIFFRACTION100
1.733-1.7890.212250.1834222X-RAY DIFFRACTION100
1.789-1.8520.2122220.1694038X-RAY DIFFRACTION100
1.852-1.9220.2072180.1623949X-RAY DIFFRACTION100
1.922-20.1761930.1633798X-RAY DIFFRACTION100
2-2.0890.1691850.1553632X-RAY DIFFRACTION100
2.089-2.1910.1881860.1583501X-RAY DIFFRACTION100
2.191-2.3090.1791800.1523305X-RAY DIFFRACTION99.9426
2.309-2.4490.1971560.1483158X-RAY DIFFRACTION99.9397
2.449-2.6170.1541540.1442954X-RAY DIFFRACTION99.9036
2.617-2.8260.1771630.1392745X-RAY DIFFRACTION99.8969
2.826-3.0940.1581300.142557X-RAY DIFFRACTION99.7032
3.094-3.4570.1731230.1422341X-RAY DIFFRACTION99.7975
3.457-3.9880.1661220.1282028X-RAY DIFFRACTION99.0783
3.988-4.8750.15770.1331770X-RAY DIFFRACTION98.9818
4.875-6.8520.201940.1821362X-RAY DIFFRACTION99.3179
6.852-44.070.165450.182828X-RAY DIFFRACTION99.2045

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more