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- PDB-1aps: THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND ST... -

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Entry
Database: PDB / ID: 1aps
TitleTHREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS
ComponentsACYLPHOSPHATASE
KeywordsHYDROLASE(ACTING ON ACID ANHYDRIDES)
Function / homology
Function and homology information


acylphosphatase / acylphosphatase activity
Similarity search - Function
Acylphosphatase signature 2. / Acylphosphatase / Acylphosphatase signature 1. / Acylphosphatase, conserved site / Acylphosphatase / Acylphosphatase-like domain / Acylphosphatase-like domain profile. / Acylphosphatase-like domain superfamily / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits ...Acylphosphatase signature 2. / Acylphosphatase / Acylphosphatase signature 1. / Acylphosphatase, conserved site / Acylphosphatase / Acylphosphatase-like domain / Acylphosphatase-like domain profile. / Acylphosphatase-like domain superfamily / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesEquus caballus (horse)
MethodSOLUTION NMR
AuthorsSaudek, V. / Pastore, A. / Ramponi, G. / Williams, R.J.P.
Citation
Journal: J.Mol.Biol. / Year: 1992
Title: Three-dimensional structure of acylphosphatase. Refinement and structure analysis.
Authors: Pastore, A. / Saudek, V. / Ramponi, G. / Williams, R.J.
#1: Journal: J.Mol.Biol. / Year: 1989
Title: Identification and Description of Beta-Structure in Horse Muscle Acylphosphatase by Nuclear Magnetic Resonance Spectroscopy
Authors: Saudek, V. / Wormald, M.R. / Williams, R.J.P. / Boyd, J. / Stefani, M. / Ramponi, G.
#2: Journal: J.Mol.Biol. / Year: 1989
Title: Identification and Description of Alpha-Helical Regions in Horse Muscle Acylphosphatase by 1H Nuclear Magnetic Resonance Spectroscopy
Authors: Saudek, V. / Atkinson, R.A. / Williams, R.J.P. / Ramponi, G.
History
DepositionFeb 20, 1991Processing site: BNL
Revision 1.0Jul 15, 1992Provider: 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: ACYLPHOSPHATASE


Theoretical massNumber of molelcules
Total (without water)11,0321
Polymers11,0321
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)5 / -
Representative

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Components

#1: Protein ACYLPHOSPHATASE


Mass: 11032.437 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equus caballus (horse) / References: UniProt: P00818, acylphosphatase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Processing

NMR ensembleConformers submitted total number: 5

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