+Open data
-Basic information
Entry | Database: PDB / ID: 1mek | ||||||
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Title | HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES | ||||||
Components | PROTEIN DISULFIDE ISOMERASEProtein disulfide-isomerase | ||||||
Keywords | ELECTRON TRANSPORT / REDOX-ACTIVE CENTER / ISOMERASE / ENDOPLASMIC RETICULUM | ||||||
Function / homology | Function and homology information regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing / procollagen-proline 4-dioxygenase activity / interleukin-23-mediated signaling pathway / LDL remodeling / thiol oxidase activity / protein disulfide-isomerase / peptidyl-proline hydroxylation to 4-hydroxy-L-proline ...regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing / procollagen-proline 4-dioxygenase activity / interleukin-23-mediated signaling pathway / LDL remodeling / thiol oxidase activity / protein disulfide-isomerase / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / endoplasmic reticulum chaperone complex / Chylomicron assembly / protein folding in endoplasmic reticulum / Collagen biosynthesis and modifying enzymes / Interleukin-23 signaling / interleukin-12-mediated signaling pathway / cellular response to interleukin-7 / Interleukin-12 signaling / Insulin processing / protein disulfide isomerase activity / Detoxification of Reactive Oxygen Species / positive regulation of cell adhesion / protein-disulfide reductase activity / endoplasmic reticulum-Golgi intermediate compartment / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of substrate adhesion-dependent cell spreading / response to endoplasmic reticulum stress / Post-translational protein phosphorylation / Hedgehog ligand biogenesis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / melanosome / integrin binding / protein folding / lamellipodium / actin binding / cellular response to hypoxia / positive regulation of viral entry into host cell / cytoskeleton / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / focal adhesion / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / extracellular exosome / extracellular region / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Kemmink, J. / Darby, N.J. / Dijkstra, K. / Nilges, M. / Creighton, T.E. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Authors: Kemmink, J. / Darby, N.J. / Dijkstra, K. / Nilges, M. / Creighton, T.E. #1: Journal: Protein Sci. / Year: 1995 Title: Nuclear Magnetic Resonance Characterization of the N-Terminal Thioredoxin-Like Domain of Protein Disulfide Isomerase Authors: Kemmink, J. / Darby, N.J. / Dijkstra, K. / Scheek, R.M. / Creighton, T.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mek.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1mek.ent.gz | 1.4 MB | Display | PDB format |
PDBx/mmJSON format | 1mek.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/me/1mek ftp://data.pdbj.org/pub/pdb/validation_reports/me/1mek | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13276.909 Da / Num. of mol.: 1 / Fragment: PROLYL 4-HYDROXYLASE BETA SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET-12 / Production host: Escherichia coli (E. coli) / References: UniProt: P07237, protein disulfide-isomerase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
Refinement | Software ordinal: 1 Details: STRUCTURES WERE DETERMINED USING A HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING APPROACH (M. NILGES, G.M. CLORE, A.M. GRONENBORN, FEBS LETT. 229, 317, 1988). THE STRUCTURES ARE BASED ON 1270 ...Details: STRUCTURES WERE DETERMINED USING A HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING APPROACH (M. NILGES, G.M. CLORE, A.M. GRONENBORN, FEBS LETT. 229, 317, 1988). THE STRUCTURES ARE BASED ON 1270 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 34 HYDROGEN BOND DISTANCE RESTRAINTS DERIVED FROM 17 SLOWLY EXCHANGING AMIDE PROTONS AND OBSERVED NOE PATTERNS; AND 5 DISTANCE RESTRAINTS WHICH DEFINE THE DISULFIDE BOND BETWEEN CYS 36 AND CYS 39. | ||||||||||||
NMR ensemble | Conformers submitted total number: 40 |