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Open data
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Basic information
Entry | Database: PDB / ID: 1mir | ||||||
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Title | RAT PROCATHEPSIN B | ||||||
![]() | PROCATHEPSIN B | ||||||
![]() | HYDROLASE / THIOL PROTEASE / CYSTEINE PROTEASE | ||||||
Function / homology | ![]() Trafficking and processing of endosomal TLR / Collagen degradation / Assembly of collagen fibrils and other multimeric structures / kininogen binding / cathepsin B / response to interleukin-4 / peptidase inhibitor complex / MHC class II antigen presentation / thyroid hormone generation / cellular response to thyroid hormone stimulus ...Trafficking and processing of endosomal TLR / Collagen degradation / Assembly of collagen fibrils and other multimeric structures / kininogen binding / cathepsin B / response to interleukin-4 / peptidase inhibitor complex / MHC class II antigen presentation / thyroid hormone generation / cellular response to thyroid hormone stimulus / proteoglycan binding / Neutrophil degranulation / response to dexamethasone / response to amine / decidualization / collagen catabolic process / response to glucose / response to mechanical stimulus / skeletal muscle tissue development / cysteine-type peptidase activity / epithelial cell differentiation / collagen binding / proteolysis involved in protein catabolic process / response to cytokine / peptide binding / protein catabolic process / response to organic cyclic compound / sarcolemma / response to peptide hormone / autophagy / cellular response to mechanical stimulus / : / melanosome / peptidase activity / spermatogenesis / neuron apoptotic process / response to ethanol / endopeptidase activity / lysosome / symbiont entry into host cell / apical plasma membrane / external side of plasma membrane / cysteine-type endopeptidase activity / protein-containing complex binding / perinuclear region of cytoplasm / cell surface / proteolysis / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Cygler, M. / Sivaraman, J. / Grochulski, P. / Coulombe, R. / Storer, A.C. / Mort, J.S. | ||||||
![]() | ![]() Title: Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Authors: Cygler, M. / Sivaraman, J. / Grochulski, P. / Coulombe, R. / Storer, A.C. / Mort, J.S. #1: ![]() Title: Crystallization of Rat Procathepsin B Authors: Sivaraman, J. / Coulombe, R. / Magny, M.-C. / Mason, P. / Mort, J.S. / Cygler, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 149.8 KB | Display | ![]() |
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PDB format | ![]() | 124.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422.4 KB | Display | ![]() |
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Full document | ![]() | 433.4 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 32.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.2123, 0.6981, -0.6839), Vector: |
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Components
#1: Protein | Mass: 35633.625 Da / Num. of mol.: 2 / Mutation: C29S, S115A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56 % |
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Crystal | *PLUS |
Crystal grow | *PLUS Method: unknown |
-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jul 7, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→74 Å / Num. obs: 19015 / % possible obs: 91 % / Observed criterion σ(I): 1 / Redundancy: 4.4 % / Rmerge(I) obs: 0.097 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 32.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.22 / Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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