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- PDB-1pcn: SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINE... -

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Entry
Database: PDB / ID: 1pcn
TitleSOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR
ComponentsPORCINE PANCREATIC PROCOLIPASE B
KeywordsLIPASE PROTEIN COFACTOR
Function / homology
Function and homology information


Digestion of dietary lipid / Retinoid metabolism and transport / lipase binding / response to food / retinoid metabolic process / lipid catabolic process / digestion / response to bacterium / enzyme activator activity / extracellular region
Similarity search - Function
Colipase / Colipase, N-terminal / Colipase, C-terminal / Colipase, conserved site / : / Colipase, N-terminal domain / Colipase, C-terminal domain / Colipase signature. / Colipase family profile. / Colipase ...Colipase / Colipase, N-terminal / Colipase, C-terminal / Colipase, conserved site / : / Colipase, N-terminal domain / Colipase, C-terminal domain / Colipase signature. / Colipase family profile. / Colipase / Lipase, subunit A / Lipase, subunit A / Ribbon / Mainly Beta
Similarity search - Domain/homology
Biological speciesSus scrofa (pig)
MethodSOLUTION NMR
AuthorsBreg, J.N. / Sarda, L. / Cozzone, P.J. / Rugani, N. / Boelens, R. / Kaptein, R.
Citation
Journal: Eur.J.Biochem. / Year: 1995
Title: Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR.
Authors: Breg, J.N. / Sarda, L. / Cozzone, P.J. / Rugani, N. / Boelens, R. / Kaptein, R.
#1: Journal: To be Published
Title: A Protein Fold Element Comprising a Triple-Strand B-Sheet and Two Disulphide Bridges Recognized in Procolipase and Other Unrelated Proteins
Authors: Breg, J.N. / Ujah, E.C. / Sarda, L. / Cozzone, P.J. / Kaptein, R.
History
DepositionJun 8, 1994Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 2.0Sep 25, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / database_PDB_caveat / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_rmsd_bond / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _atom_site.auth_atom_id / _atom_site.auth_comp_id ..._atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.group_PDB / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_assembly_gen.asym_id_list
Revision 2.1Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure viewerMolecule:
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Assembly

Deposited unit
A: PORCINE PANCREATIC PROCOLIPASE B


Theoretical massNumber of molelcules
Total (without water)10,1171
Polymers10,1171
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein PORCINE PANCREATIC PROCOLIPASE B


Mass: 10117.486 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P02703
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 ensembleConformers submitted total number: 1

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