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- PDB-1rou: STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BI... -

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Basic information

Entry
Database: PDB / ID: 1rou
TitleSTRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, 22 STRUCTURES
ComponentsFKBP59-I
KeywordsROTAMASE (ISOMERASE) / DOMAIN I (N-TERM) OF A 59 KDA / FK506-BINDING PROTEIN / PEPTIDYL PROLYL CIS-TRANS ISOMERASE
Function / homology
Function and homology information


negative regulation of microtubule polymerization or depolymerization / axonal growth cone / chaperone-mediated protein folding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / tau protein binding / negative regulation of neuron projection development / microtubule / mitochondrion / nucleus / cytosol
Similarity search - Function
Tetratricopeptide repeat 2 / Tetratricopeptide repeat / : / Chitinase A; domain 3 - #40 / Tetratricopeptide repeat / Chitinase A; domain 3 / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily ...Tetratricopeptide repeat 2 / Tetratricopeptide repeat / : / Chitinase A; domain 3 - #40 / Tetratricopeptide repeat / Chitinase A; domain 3 / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Peptidyl-prolyl cis-trans isomerase FKBP4
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
MethodSOLUTION NMR
AuthorsCraescu, C.T. / Rouviere, N. / Popescu, A. / Cerpolini, E. / Lebeau, M.-C. / Baulieu, E.-E. / Mispelter, J.
Citation
Journal: Biochemistry / Year: 1996
Title: Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution.
Authors: Craescu, C.T. / Rouviere, N. / Popescu, A. / Cerpolini, E. / Lebeau, M.C. / Baulieu, E.E. / Mispelter, J.
#1: Journal: Eur.J.Biochem. / Year: 1995
Title: 1H and 15N Assignment of NMR Spectrum, Secondary Structure and Global Folding of the Immunophilin-Like Domain of the 59-kDa Fk506-Binding Protein
Authors: Rouviere-Fourmy, N. / Craescu, C.T. / Mispelter, J. / Lebeau, M.C. / Baulieu, E.E.
History
DepositionJun 14, 1996Processing site: BNL
Revision 1.0Dec 7, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
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: FKBP59-I


Theoretical massNumber of molelcules
Total (without water)16,2591
Polymers16,2591
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)22 / -
Representative

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Components

#1: Protein FKBP59-I / FKBP52 OR HSP56


Mass: 16259.305 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Organ: LIVER / Production host: Escherichia coli (E. coli) / References: UniProt: P27124

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 6.7 / Temperature units: K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: Discover / Developer: BIOSYM / Classification: refinement
RefinementSoftware ordinal: 1 / Details: CVFF OF DISCOVER (BIOSYM)
NMR ensembleConformers submitted total number: 22

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