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- PDB-2vki: Structure of the PDK1 PH domain K465E mutant -

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Basic information

Entry
Database: PDB / ID: 2vki
TitleStructure of the PDK1 PH domain K465E mutant
Components3-PHOPSHOINOSITIDE DEPENDENT PROTEIN KINASE 1
KeywordsTRANSFERASE / PLECKSTRIN HOMOLOGY / CANCER / DIABETES
Function / homology
Function and homology information


intracellular signaling cassette / 3-phosphoinositide-dependent protein kinase activity / Activation of AKT2 / regulation of mast cell degranulation / type B pancreatic cell development / negative regulation of toll-like receptor signaling pathway / RSK activation / positive regulation of vascular endothelial cell proliferation / regulation of canonical NF-kappaB signal transduction / phospholipase activator activity ...intracellular signaling cassette / 3-phosphoinositide-dependent protein kinase activity / Activation of AKT2 / regulation of mast cell degranulation / type B pancreatic cell development / negative regulation of toll-like receptor signaling pathway / RSK activation / positive regulation of vascular endothelial cell proliferation / regulation of canonical NF-kappaB signal transduction / phospholipase activator activity / positive regulation of sprouting angiogenesis / Constitutive Signaling by AKT1 E17K in Cancer / negative regulation of endothelial cell apoptotic process / negative regulation of cardiac muscle cell apoptotic process / Role of LAT2/NTAL/LAB on calcium mobilization / CD28 dependent PI3K/Akt signaling / positive regulation of blood vessel endothelial cell migration / extrinsic apoptotic signaling pathway / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / T cell costimulation / vascular endothelial cell response to laminar fluid shear stress / Estrogen-stimulated signaling through PRKCZ / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / GPVI-mediated activation cascade / insulin-like growth factor receptor signaling pathway / phospholipase binding / Integrin signaling / cell projection / cellular response to epidermal growth factor stimulus / positive regulation of release of sequestered calcium ion into cytosol / negative regulation of transforming growth factor beta receptor signaling pathway / phosphatidylinositol 3-kinase/protein kinase B signal transduction / VEGFR2 mediated vascular permeability / VEGFR2 mediated cell proliferation / calcium-mediated signaling / positive regulation of protein localization to plasma membrane / insulin receptor signaling pathway / epidermal growth factor receptor signaling pathway / CLEC7A (Dectin-1) signaling / positive regulation of angiogenesis / FCERI mediated NF-kB activation / actin cytoskeleton organization / cellular response to insulin stimulus / Regulation of TP53 Degradation / PIP3 activates AKT signaling / protein autophosphorylation / Downstream TCR signaling / cell migration / G beta:gamma signalling through PI3Kgamma / cytoplasmic vesicle / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein phosphorylation / non-specific serine/threonine protein kinase / postsynaptic density / intracellular signal transduction / protein serine kinase activity / focal adhesion / protein serine/threonine kinase activity / DNA-templated transcription / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
PDK1-type, PH domain / PH domain / PDPK1 family / : / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / PH-like domain superfamily / Roll / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. ...PDK1-type, PH domain / PH domain / PDPK1 family / : / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / PH-like domain superfamily / Roll / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta
Similarity search - Domain/homology
3-phosphoinositide-dependent protein kinase 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsKomander, D. / Bayascas, J.R. / Deak, M. / Alessi, D.R. / van Aalten, D.M.F.
CitationJournal: Mol.Cell.Biol. / Year: 2008
Title: Mutation of the Pdk1 Ph Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance.
Authors: Bayascas, J.R. / Wullschleger, S. / Sakamoto, K. / Garcia-Martinez, J.M. / Clacher, C. / Komander, D. / Van Aalten, D.M.F. / Boini, K.M. / Lang, F. / Lipina, C. / Logie, L. / Sutherland, C. ...Authors: Bayascas, J.R. / Wullschleger, S. / Sakamoto, K. / Garcia-Martinez, J.M. / Clacher, C. / Komander, D. / Van Aalten, D.M.F. / Boini, K.M. / Lang, F. / Lipina, C. / Logie, L. / Sutherland, C. / Chudek, J.A. / Van Diepen, J.A. / Voshol, P.J. / Lucocq, J.M. / Alessi, D.R.
History
DepositionDec 19, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 13, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 3-PHOPSHOINOSITIDE DEPENDENT PROTEIN KINASE 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,7373
Polymers17,5491
Non-polymers1882
Water2,018112
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)34.009, 67.057, 67.802
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein 3-PHOPSHOINOSITIDE DEPENDENT PROTEIN KINASE 1 / HPDK1


Mass: 17548.791 Da / Num. of mol.: 1 / Fragment: PLECKSTRIN HOMOLOGY (PH) DOMAIN, RESIDUES 409-556 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX6P1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O15530, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 112 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN A, LYS 465 TO GLU
Sequence detailsPOINT MUTATION K465E

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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: 2.2 Å3/Da / Density % sol: 44 % / Description: NONE
Crystal growpH: 8.5
Details: 0.2 M LITHIUM SULPHATE, 0.1 M TRIS HYDROCHLORIDE [PH 8.5] 30 % (W/V) PEG 4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418
DetectorType: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Jun 30, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.8→25 Å / Num. obs: 14950 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 4.5 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 10
Reflection shellResolution: 1.8→1.86 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.3 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1W1D

1w1d


Resolution: 1.8→25 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.952 / SU B: 2.765 / SU ML: 0.084 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.121 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED RESIDUES WERE MODELLED AS ALA OR WITH OCCU 0.01. THE C-TERMINUS IS DISORDERED.
RfactorNum. reflection% reflectionSelection details
Rfree0.215 609 4.1 %RANDOM
Rwork0.173 ---
obs0.175 14309 99.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 21.05 Å2
Baniso -1Baniso -2Baniso -3
1-0.12 Å20 Å20 Å2
2---0.64 Å20 Å2
3---0.52 Å2
Refinement stepCycle: LAST / Resolution: 1.8→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1172 0 11 112 1295
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0211242
X-RAY DIFFRACTIONr_bond_other_d0.0020.021101
X-RAY DIFFRACTIONr_angle_refined_deg1.6811.9441677
X-RAY DIFFRACTIONr_angle_other_deg0.90432566
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.2985138
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1060.2170
X-RAY DIFFRACTIONr_gen_planes_refined0.010.021354
X-RAY DIFFRACTIONr_gen_planes_other0.0110.02271
X-RAY DIFFRACTIONr_nbd_refined0.2160.2215
X-RAY DIFFRACTIONr_nbd_other0.2530.21257
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0860.2730
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.160.289
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.190.217
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3120.279
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1170.212
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9831.5700
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.7821137
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.5423542
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.0594.5540
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
LS refinement shellResolution: 1.8→1.84 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.348 45
Rwork0.268 1000
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)
10.3314-0.15150.12281.1483-0.13520.8004-0.003-0.0485-0.00110.03060.0445-0.0373-0.02510.0218-0.04150.0395-0.0056-0.00720.0345-0.00870.04281.970317.696311.186
20.5356-0.26010.12610.2234-0.0011.0095-0.0394-0.06790.02860.00220.04070.02280.0028-0.0211-0.00130.01170.008-0.00760.0128-0.02090.0388-0.746916.304912.3078
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A414 - 466
2X-RAY DIFFRACTION1A472 - 487
3X-RAY DIFFRACTION1A494 - 543
4X-RAY DIFFRACTION2A410 - 413
5X-RAY DIFFRACTION2A467 - 471
6X-RAY DIFFRACTION2A544 - 549
7X-RAY DIFFRACTION2A488 - 493

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