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- PDB-2crd: ANALYSIS OF SIDE-CHAIN ORGANIZATION ON A REFINED MODEL OF CHARYBD... -

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Basic information

Entry
Database: PDB / ID: 2crd
TitleANALYSIS OF SIDE-CHAIN ORGANIZATION ON A REFINED MODEL OF CHARYBDOTOXIN: STRUCTURAL AND FUNCTIONAL IMPLICATIONS
ComponentsCHARYBDOTOXIN
KeywordsNEUROTOXIN
Function / homology
Function and homology information


ion channel inhibitor activity / defense response to fungus / potassium channel regulator activity / toxin activity / killing of cells of another organism / defense response to bacterium / extracellular region
Similarity search - Function
Scorpion short toxins signature. / Scorpion short chain toxin, potassium channel inhibitor / Scorpion short toxin, BmKK2 / Knottin, scorpion toxin-like superfamily
Similarity search - Domain/homology
Potassium channel toxin alpha-KTx 1.1
Similarity search - Component
Biological speciesLeiurus quinquestriatus hebraeus (scorpion)
MethodSOLUTION NMR
AuthorsBontems, F. / Roumestand, C. / Gilquin, B. / Menez, A. / Toma, F.
Citation
Journal: Biochemistry / Year: 1992
Title: Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications.
Authors: Bontems, F. / Gilquin, B. / Roumestand, C. / Menez, A. / Toma, F.
#1: Journal: Science / Year: 1991
Title: Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins
Authors: Bontems, F. / Roumestand, C. / Gilquin, B. / Menez, A. / Toma, F.
History
DepositionFeb 17, 1993Processing site: BNL
Revision 1.0Jul 15, 1993Provider: 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 2.0Dec 25, 2019Group: Derived calculations / Polymer sequence
Category: entity_poly / pdbx_struct_mod_residue / struct_conn
Item: _entity_poly.pdbx_seq_one_letter_code_can / _pdbx_struct_mod_residue.parent_comp_id / _struct_conn.pdbx_leaving_atom_flag
Revision 2.1Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CHARYBDOTOXIN


Theoretical massNumber of molelcules
Total (without water)4,3101
Polymers4,3101
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)12 / -
Representative

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Components

#1: Protein/peptide CHARYBDOTOXIN


Mass: 4309.998 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Leiurus quinquestriatus hebraeus (scorpion)
Species: Leiurus quinquestriatus / Strain: hebraeus / References: UniProt: P13487
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

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 12

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