+Open data
-Basic information
Entry | Database: PDB / ID: 1gd3 | ||||||
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Title | refined solution structure of human cystatin A | ||||||
Components | CYSTATIN A | ||||||
Keywords | PROTEIN BINDING / cystatin A / Thiol protease inhibitor | ||||||
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 / distance geometry, simulated annealing | ||||||
Authors | Shimba, N. / Kariya, E. / Tate, S. / Kaji, H. / Kainosho, M. | ||||||
Citation | Journal: J.STRUCT.FUNCT.GENOM. / Year: 2000 Title: Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the a-helix conformation ? Authors: Shimba, N. / Kariya, E. / Tate, S. / Kaji, H. / Kainosho, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gd3.cif.gz | 43.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gd3.ent.gz | 32.1 KB | Display | PDB format |
PDBx/mmJSON format | 1gd3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gd/1gd3 ftp://data.pdbj.org/pub/pdb/validation_reports/gd/1gd3 | 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: 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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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0 / pH: 4.0 / Pressure: ambient / Temperature: 310 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz |
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-Processing
NMR software | Name: X-PLOR / Version: 3.85 / Classification: refinement |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 |
NMR ensemble | Conformers submitted total number: 1 |