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- PDB-1dvc: SOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR,... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dvc | ||||||
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Title | SOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
![]() | STEFIN A | ||||||
![]() | THIOL PROTEASE INHIBITOR | ||||||
Function / homology | ![]() 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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Martin, J.R. / Craven, C.J. / Jerala, R. / Kroon-Zitko, L. / Zerovnik, E. / Turk, V. / Waltho, J.P. | ||||||
![]() | ![]() 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: ![]() 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 43.7 KB | Display | ![]() |
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PDB format | ![]() | 31.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 242.4 KB | Display | ![]() |
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Full document | ![]() | 242.1 KB | Display | |
Data in XML | ![]() | 4.5 KB | Display | |
Data in CIF | ![]() | 5.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 11020.464 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 5.5 / Temperature: 308 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |