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- PDB-2ech: ECHISTATIN-THE REFINED STRUCTURE OF A DISINTEGRIN IN SOLUTION BY ... -

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Basic information

Entry
Database: PDB / ID: 2ech
TitleECHISTATIN-THE REFINED STRUCTURE OF A DISINTEGRIN IN SOLUTION BY 1H NMR
ComponentsECHISTATIN
KeywordsBLOOD COAGULATION INHIBITOR
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / metalloendopeptidase activity / toxin activity / proteolysis / extracellular region / metal ion binding
Similarity search - Function
Disintegrin domain / Echistatin / Disintegrin, conserved site / Disintegrins signature. / Reprolysin domain, adamalysin-type / Reprolysin (M12B) family zinc metalloprotease / Disintegrin / Disintegrin domain profile. / Homologues of snake disintegrins / Disintegrin domain ...Disintegrin domain / Echistatin / Disintegrin, conserved site / Disintegrins signature. / Reprolysin domain, adamalysin-type / Reprolysin (M12B) family zinc metalloprotease / Disintegrin / Disintegrin domain profile. / Homologues of snake disintegrins / Disintegrin domain / Disintegrin domain superfamily / Peptidase M12B, ADAM/reprolysin / ADAM type metalloprotease domain profile. / Metallopeptidase, catalytic domain superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Disintegrin metalloproteinase/disintegrin echistatin
Similarity search - Component
Biological speciesEchis carinatus (saw-scaled viper)
MethodSOLUTION NMR
AuthorsPelton, J.T. / Atkinson, R.A. / Saudek, V.
Citation
Journal: Int.J.Pept.Protein Res. / Year: 1994
Title: Echistatin: the refined structure of a disintegrin in solution by 1H NMR and restrained molecular dynamics.
Authors: Atkinson, R.A. / Saudek, V. / Pelton, J.T.
#1: Journal: Eur.J.Biochem. / Year: 1991
Title: The Secondary Structure of Echistatin from 1H-NMR, Circular-Dichroism and Raman Spectroscopy
Authors: Saudek, V. / Atkinson, R.A. / Lepage, P. / Pelton, J.T.
#2: Journal: Biochemistry / Year: 1991
Title: Three-Dimensional Structure of Echistatin, the Smallest Active Rgd Protein
Authors: Saudek, V. / Atkinson, R.A. / Pelton, J.T.
History
DepositionApr 13, 1993Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 3, 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
Item: _pdbx_database_status.process_site
Revision 1.4Oct 16, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _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: ECHISTATIN


Theoretical massNumber of molelcules
Total (without water)5,4331
Polymers5,4331
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)8 / -
Representative

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Components

#1: Protein/peptide ECHISTATIN


Mass: 5433.197 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Echis carinatus (saw-scaled viper) / References: UniProt: P17347
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: 8

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