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- PDB-1sfv: PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE -

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Basic information

Entry
Database: PDB / ID: 1sfv
TitlePORCINE PANCREAS PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsPHOSPHOLIPASE A2
KeywordsHYDROLASE / PHOSPHOLIPASE A2 / PHOSPHATIDE-2-ACYL-HYDROLASE
Function / homology
Function and homology information


positive regulation of podocyte apoptotic process / regulation of D-glucose import / phospholipase A2 activity / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process / leukotriene biosynthetic process / neutrophil mediated immunity / phospholipase A2 / bile acid binding / calcium-dependent phospholipase A2 activity ...positive regulation of podocyte apoptotic process / regulation of D-glucose import / phospholipase A2 activity / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process / leukotriene biosynthetic process / neutrophil mediated immunity / phospholipase A2 / bile acid binding / calcium-dependent phospholipase A2 activity / positive regulation of calcium ion transport into cytosol / lipid catabolic process / neutrophil chemotaxis / positive regulation of MAP kinase activity / positive regulation of interleukin-8 production / positive regulation of immune response / phospholipid binding / cellular response to insulin stimulus / positive regulation of fibroblast proliferation / fatty acid biosynthetic process / positive regulation of MAPK cascade / intracellular signal transduction / signaling receptor binding / positive regulation of cell population proliferation / calcium ion binding / cell surface / positive regulation of transcription by RNA polymerase II / extracellular region
Similarity search - Function
Phospholipase A2, aspartic acid active site / Phospholipase A2 aspartic acid active site. / Phospholipase A2 / Phospholipase A2 / Phospholipase A2, histidine active site / Phospholipase A2 histidine active site. / Phospholipase A2 domain / Phospholipase A2 / Phospholipase A2 / Phospholipase A2 domain ...Phospholipase A2, aspartic acid active site / Phospholipase A2 aspartic acid active site. / Phospholipase A2 / Phospholipase A2 / Phospholipase A2, histidine active site / Phospholipase A2 histidine active site. / Phospholipase A2 domain / Phospholipase A2 / Phospholipase A2 / Phospholipase A2 domain / Phospholipase A2 domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Phospholipase A2, major isoenzyme
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodSOLUTION NMR
AuthorsVan Den Berg, B. / Tessari, M. / Boelens, R. / Dijkman, R. / Kaptein, R. / De Haas, G.H. / Verheij, H.M.
Citation
Journal: J.Biomol.NMR / Year: 1995
Title: Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor.
Authors: van den Berg, B. / Tessari, M. / Boelens, R. / Dijkman, R. / Kaptein, R. / de Haas, G.H. / Verheij, H.M.
#1: Journal: Embo J. / Year: 1995
Title: Solution Structure of Porcine Pancreatic Phospholipase A2
Authors: Van Den Berg, B. / Tessari, M. / De Haas, G.H. / Verheij, H.M. / Boelens, R. / Kaptein, R.
#2: Journal: Nat.Struct.Biol. / Year: 1995
Title: NMR Structures of Phospholipase A2 Reveal Conformational Changes During Interfacial Activation
Authors: Van Den Berg, B. / Tessari, M. / Boelens, R. / Dijkman, R. / De Haas, G.H. / Kaptein, R. / Verheij, H.M.
History
DepositionFeb 20, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / 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_nmr_software.name / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_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
Revision 1.4Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: PHOSPHOLIPASE A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,0502
Polymers14,0101
Non-polymers401
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein PHOSPHOLIPASE A2 / PLA2 / PHOSPHATIDYLCHOLINE 2-ACYLHYDROLASE


Mass: 14009.714 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: THIS ENTRY PRESENTS THE SOLUTION STRUCTURE OF THE ENZYME IN THE PRESENCE OF LIPID MICELLES AND A COMPETITIVE INHIBITOR
Source: (gene. exp.) Sus scrofa (pig)
Description: DETAILS CONCERNING THE EXPRESSION OF THE PLA2 CAN BE FOUND IN REFERENCES BELOW
Gene: PORCINE PANCREAS PLA2 / Organ: PANCREAS / Plasmid: PAB3 (PGEX T2 DERIVED EXPRESSION PLASMID) / Gene (production host): PORCINE PANCREAS PLA2 / Production host: Escherichia coli (E. coli) / References: UniProt: P00592, phospholipase A2
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: Discover / Developer: BIOSYM / Classification: refinement
NMR ensembleConformers submitted total number: 1

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