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Yorodumi- PDB-1cyu: SOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cyu | ||||||
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Title | SOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE CONDITION OF PH 3.8 AND 310K | ||||||
Components | CYSTATIN A | ||||||
Keywords | PROTEINASE INHIBITOR (CYSTEINE) | ||||||
Function / homology | Function and homology information negative regulation of peptidase activity / peptidase inhibitor complex / Formation of the cornified envelope / peptide cross-linking / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation / negative regulation of proteolysis / cell-cell adhesion / protease binding ...negative regulation of peptidase activity / peptidase inhibitor complex / Formation of the cornified envelope / peptide cross-linking / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation / negative regulation of proteolysis / cell-cell adhesion / protease binding / extracellular space / nucleoplasm / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Tate, S. / Tate, N.U. / Ushioda, T. / Samejima, T. / Kainosho, M. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A. Authors: Tate, S. / Ushioda, T. / Utsunomiya-Tate, N. / Shibuya, K. / Ohyama, Y. / Nakano, Y. / Kaji, H. / Inagaki, F. / Samejima, T. / Kainosho, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cyu.cif.gz | 458.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cyu.ent.gz | 379.2 KB | Display | PDB format |
PDBx/mmJSON format | 1cyu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cy/1cyu ftp://data.pdbj.org/pub/pdb/validation_reports/cy/1cyu | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11002.426 Da / Num. of mol.: 1 / Mutation: DEL(M1), M65L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01040 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
NMR ensemble | Conformers submitted total number: 15 |