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- PDB-1dvc: SOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR,... -

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Basic information

Entry
Database: PDB / ID: 1dvc
TitleSOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsSTEFIN A
KeywordsTHIOL PROTEASE INHIBITOR
Function / homology
Function and homology information


peptidase inhibitor complex / peptide cross-linking / Formation of the cornified envelope / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation / negative regulation of proteolysis / cell-cell adhesion / protease binding / extracellular space ...peptidase inhibitor complex / peptide cross-linking / Formation of the cornified envelope / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation / negative regulation of proteolysis / cell-cell adhesion / protease binding / extracellular space / nucleoplasm / cytoplasm / cytosol
Similarity search - Function
Proteinase inhibitor I25A, stefin / Proteinase inhibitor I25, cystatin, conserved site / Cysteine proteases inhibitors signature. / Cystatin domain / Cystatin-like domain / Cystatin domain / Nuclear Transport Factor 2; Chain: A, - #10 / Cystatin superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsMartin, J.R. / Craven, C.J. / Jerala, R. / Kroon-Zitko, L. / Zerovnik, E. / Turk, V. / Waltho, J.P.
Citation
Journal: J.Mol.Biol. / Year: 1995
Title: The three-dimensional solution structure of human stefin A.
Authors: Martin, J.R. / Craven, C.J. / Jerala, R. / Kroon-Zitko, L. / Zerovnik, E. / Turk, V. / Waltho, J.P.
#1: Journal: Eur.J.Biochem. / Year: 1994
Title: Structural Characterisation of Human Stefin a in Solution and Implications for Binding to Cysteine Proteinases
Authors: Martin, J.R. / Jerala, R. / Kroon-Zitko, L. / Zerovnik, E. / Turk, V. / Waltho, J.P.
History
DepositionFeb 26, 1996Processing site: BNL
Revision 1.0Aug 1, 1996Provider: 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: STEFIN A


Theoretical massNumber of molelcules
Total (without water)11,0201
Polymers11,0201
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)1 / -
Representative

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Components

#1: Protein STEFIN A / CYSTATIN A


Mass: 11020.464 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / Plasmid: PKP1500 / Production host: Escherichia coli (E. coli) / References: UniProt: P01040

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 1

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