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- PDB-1bvh: SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHO... -

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Basic information

Entry
Database: PDB / ID: 1bvh
TitleSOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE
ComponentsACID PHOSPHATASE
KeywordsHYDROLASE
Function / homology
Function and homology information


acid phosphatase / acid phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / cytoplasm
Similarity search - Function
Protein-tyrosine phosphatase, low molecular weight, mammalian / : / Protein-tyrosine phosphatase, low molecular weight / Phosphotyrosine protein phosphatase I / Phosphotyrosine protein phosphatase I superfamily / Low molecular weight phosphotyrosine protein phosphatase / Low molecular weight phosphatase family / Response regulator / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Low molecular weight phosphotyrosine protein phosphatase
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodSOLUTION NMR
AuthorsLogan, T.M. / Zhou, M.-M. / Nettesheim, D.G. / Meadows, R.P. / Van Etten, R.L. / Fesik, S.W.
Citation
Journal: Biochemistry / Year: 1994
Title: Solution structure of a low molecular weight protein tyrosine phosphatase.
Authors: Logan, T.M. / Zhou, M.M. / Nettesheim, D.G. / Meadows, R.P. / Van Etten, R.L. / Fesik, S.W.
#1: Journal: Biochemistry / Year: 1994
Title: Backbone 1H, 13C, and 15N Assignments and Secondary Structure of Bovine Low-Molecular-Weight Phosphotyrosyl Protein Phosphatase
Authors: Zhou, M.-M. / Logan, T.M. / Theriault, Y. / Van Etten, R.L. / Fesik, S.W.
History
DepositionMay 3, 1994Processing site: BNL
Revision 1.0Jul 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ACID PHOSPHATASE


Theoretical massNumber of molelcules
Total (without water)17,9461
Polymers17,9461
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)15 / -
Representative

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Components

#1: Protein ACID PHOSPHATASE


Mass: 17946.326 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Organ: HEART / Production host: Escherichia coli (E. coli) / References: UniProt: P11064, acid phosphatase

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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: 15

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