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- PDB-1ptq: PROTEIN KINASE C DELTA CYS2 DOMAIN -

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Basic information

Entry
Database: PDB / ID: 1ptq
TitlePROTEIN KINASE C DELTA CYS2 DOMAIN
ComponentsPROTEIN KINASE C DELTA TYPE
KeywordsPHOSPHOTRANSFERASE
Function / homology
Function and homology information


DAG and IP3 signaling / positive regulation of phospholipid scramblase activity / positive regulation of glucosylceramide catabolic process / positive regulation of sphingomyelin catabolic process / Apoptotic cleavage of cellular proteins / SHC1 events in ERBB2 signaling / VEGFR2 mediated cell proliferation / regulation of ceramide biosynthetic process / Interferon gamma signaling / Effects of PIP2 hydrolysis ...DAG and IP3 signaling / positive regulation of phospholipid scramblase activity / positive regulation of glucosylceramide catabolic process / positive regulation of sphingomyelin catabolic process / Apoptotic cleavage of cellular proteins / SHC1 events in ERBB2 signaling / VEGFR2 mediated cell proliferation / regulation of ceramide biosynthetic process / Interferon gamma signaling / Effects of PIP2 hydrolysis / HuR (ELAVL1) binds and stabilizes mRNA / phospholipase C/protein kinase C signal transduction / TIR domain binding / negative regulation of filopodium assembly / Calmodulin induced events / protein kinase C signaling / calcium,diacylglycerol-dependent serine/threonine kinase activity / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / endolysosome / positive regulation of ceramide biosynthetic process / Role of phospholipids in phagocytosis / diacylglycerol-dependent serine/threonine kinase activity / termination of signal transduction / cellular response to hydroperoxide / protein kinase C / RHO GTPases Activate NADPH Oxidases / negative regulation of actin filament polymerization / collagen metabolic process / negative regulation of glial cell apoptotic process / CLEC7A (Dectin-1) signaling / neutrophil activation / regulation of phosphorylation / D-aspartate import across plasma membrane / negative regulation of platelet aggregation / B cell proliferation / immunoglobulin mediated immune response / peptidyl-threonine phosphorylation / positive regulation of MAP kinase activity / cellular response to angiotensin / insulin receptor substrate binding / postsynaptic cytosol / protein tyrosine kinase activator activity / negative regulation of MAPK cascade / positive regulation of superoxide anion generation / negative regulation of insulin receptor signaling pathway / Neutrophil degranulation / positive regulation of D-glucose import across plasma membrane / endomembrane system / positive regulation of apoptotic signaling pathway / post-translational protein modification / negative regulation of smoothened signaling pathway / positive regulation of DNA repair / regulation of actin cytoskeleton organization / protein serine/threonine kinase binding / non-specific protein-tyrosine kinase / cell chemotaxis / positive regulation of protein import into nucleus / non-membrane spanning protein tyrosine kinase activity / negative regulation of inflammatory response / peptidyl-serine phosphorylation / cellular senescence / cellular response to hydrogen peroxide / enzyme activator activity / nuclear matrix / cellular response to UV / cell-cell junction / protein autophosphorylation / cellular response to oxidative stress / response to oxidative stress / positive regulation of MAPK cascade / defense response to bacterium / protein kinase activity / protein phosphorylation / intracellular signal transduction / positive regulation of apoptotic process / apoptotic process / protein serine kinase activity / protein serine/threonine kinase activity / DNA damage response / protein kinase binding / perinuclear region of cytoplasm / Golgi apparatus / enzyme binding / endoplasmic reticulum / mitochondrion / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Protein kinase C, delta / Protein kinase C delta/epsilon/eta/theta, C2 domain / Protein kinase C, delta/epsilon/eta/theta types / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #20 / Protein kinase, C-terminal / Protein kinase C terminal domain / Wheat Germ Agglutinin (Isolectin 2); domain 1 / Diacylglycerol/phorbol-ester binding / Phorbol esters/diacylglycerol binding domain (C1 domain) / Zinc finger phorbol-ester/DAG-type signature. ...Protein kinase C, delta / Protein kinase C delta/epsilon/eta/theta, C2 domain / Protein kinase C, delta/epsilon/eta/theta types / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #20 / Protein kinase, C-terminal / Protein kinase C terminal domain / Wheat Germ Agglutinin (Isolectin 2); domain 1 / Diacylglycerol/phorbol-ester binding / Phorbol esters/diacylglycerol binding domain (C1 domain) / Zinc finger phorbol-ester/DAG-type signature. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C2 domain / C2 domain profile. / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / C2 domain superfamily / 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 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Protein kinase C delta type
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.95 Å
AuthorsZhang, G. / Hurley, J.H.
CitationJournal: Cell(Cambridge,Mass.) / Year: 1995
Title: Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester.
Authors: Zhang, G. / Kazanietz, M.G. / Blumberg, P.M. / Hurley, J.H.
History
DepositionMay 11, 1995Processing site: BNL
Revision 1.0Jul 31, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_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

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Assembly

Deposited unit
A: PROTEIN KINASE C DELTA TYPE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)5,9433
Polymers5,8121
Non-polymers1312
Water00
1
A: PROTEIN KINASE C DELTA TYPE
hetero molecules

A: PROTEIN KINASE C DELTA TYPE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,8856
Polymers11,6242
Non-polymers2624
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_566x,-y+1,-z+11
Unit cell
Length a, b, c (Å)32.400, 63.500, 65.500
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein/peptide PROTEIN KINASE C DELTA TYPE


Mass: 5811.855 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX / Production host: Escherichia coli (E. coli)
References: UniProt: P28867, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.9 Å3/Da / Density % sol: 57.55 %
Crystal grow
*PLUS
Temperature: 4 ℃ / pH: 6.8 / Method: vapor diffusion, hanging drop / Details: used as seeds
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
18 mg/mlprotein1drop
255 %ammonium sulfate1drop
30.1 Mphosphate1drop
41 mMDTT1drop
525 %isopropanol1reservoir
60.2 Mammonium acetate1reservoir
70.1 Msodium phosphate1reservoir

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Data collection

Diffraction
IDCrystal-ID
11
21
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONNSLS X4A11.2826,1.2818,1.2613
ROTATING ANODE21.5418
Detector
TypeIDDetectorDate
FUJI1IMAGE PLATEOct 29, 1994
RIGAKU RAXIS II2IMAGE PLATESep 5, 1994
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1MADMx-ray1
2SINGLE WAVELENGTHMx-ray2
Radiation wavelength
IDWavelength (Å)Relative weight
11.28261
21.28181
31.26131
41.54181
ReflectionResolution: 1.95→20 Å / Num. obs: 4073 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 8 % / Rmerge(I) obs: 0.06
Reflection
*PLUS
Rmerge(I) obs: 0.06

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
DENZOdata reduction
X-PLOR3.1phasing
RefinementResolution: 1.95→6 Å / σ(F): 0 /
RfactorNum. reflection
Rwork0.196 -
obs0.196 4073
Displacement parametersBiso mean: 16.3 Å2
Refinement stepCycle: LAST / Resolution: 1.95→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms402 0 2 0 404
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg2.9
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refine LS restraints
*PLUS
Type: x_bond_d / Dev ideal: 0.014

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