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- PDB-1evc: NMR structure of CYANOBACTERIAL TOXIN, PHOSPHATASE-1/-2A INHIBITOR -

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Basic information

Entry
Database: PDB / ID: 1evc
TitleNMR structure of CYANOBACTERIAL TOXIN, PHOSPHATASE-1/-2A INHIBITOR
ComponentsMOTUPORIN
KeywordsHYDROLASE INHIBITOR / TOXIN / CYANOBACTERIAL TOXIN / PHOSPHATASE-1/-2A INHIBITOR
Function / homologymotuporin / :
Function and homology information
Biological speciesunidentified (others)
MethodSOLUTION NMR
AuthorsBagu, J.R. / Sykes, B.D.
Citation
Journal: Nat.Struct.Biol. / Year: 1995
Title: Comparison of the solution structures of microcystin-LR and motuporin.
Authors: Bagu, J.R. / Sonnichsen, F.D. / Williams, D. / Andersen, R.J. / Sykes, B.D. / Holmes, C.F.
#1: Journal: Curr.Opin.Struct.Biol. / Year: 1993
Title: Inhibitors of Protein Phosphatase-1 and-2A; Two of Major Serine/Threonine Protein Phosphatases Involved in Cellular Regulation
Authors: Holmes, C.F.B. / Boland, M.P.
History
DepositionFeb 14, 1996Processing site: BNL
Revision 1.0Nov 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Version format compliance
Revision 1.3Jul 27, 2011Group: Database references
Revision 1.4Dec 12, 2012Group: Other
Revision 1.5Jun 24, 2020Group: Advisory / Database references ...Advisory / Database references / Derived calculations / Other
Category: pdbx_database_related / pdbx_database_status ...pdbx_database_related / pdbx_database_status / pdbx_validate_polymer_linkage / struct_conn
Item: _pdbx_database_related.content_type / _pdbx_database_status.process_site
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle / struct_conn
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MOTUPORIN


Theoretical massNumber of molelcules
Total (without water)7861
Polymers7861
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)48 / -
Representative

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Components

#1: Protein/peptide MOTUPORIN / NODULARIN-V


Type: Cyclic peptide / Class: Toxin / Mass: 785.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM MARINE SPONGE / Source: (natural) unidentified (others) / References: NOR: NOR00825, motuporin

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 7 / Temperature: 278 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: DGII / Developer: HAVEL / Classification: refinement
NMR ensembleConformers submitted total number: 48

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