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Open data
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Basic information
Entry | Database: PDB / ID: 3cw1 | ||||||
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Title | Crystal Structure of Human Spliceosomal U1 snRNP | ||||||
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![]() | SPLICING / pre-mRNA splicing / spliceosome / RNA-binding domain / Sm fold / zinc finger / RNA recognition motif / 5' splice site | ||||||
Function / homology | ![]() negative regulation of protein refolding / regulation of ATP-dependent activity / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / histone pre-mRNA 3'end processing complex / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / protein methylation ...negative regulation of protein refolding / regulation of ATP-dependent activity / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / histone pre-mRNA 3'end processing complex / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / protein methylation / U12-type spliceosomal complex / methylosome / 7-methylguanosine cap hypermethylation / U1 snRNP binding / pICln-Sm protein complex / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / P granule / telomerase holoenzyme complex / negative regulation of chaperone-mediated autophagy / U2-type spliceosomal complex / U2-type precatalytic spliceosome / commitment complex / telomerase RNA binding / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / U4 snRNP / U2 snRNP / positive regulation of mRNA splicing, via spliceosome / RNA Polymerase II Transcription Termination / U1 snRNP / pre-mRNA 5'-splice site binding / U2-type prespliceosome / precatalytic spliceosome / spliceosomal complex assembly / mRNA Splicing - Minor Pathway / mRNA 5'-splice site recognition / regulation of RNA splicing / U5 snRNP / spliceosomal snRNP assembly / Cajal body / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / spliceosomal complex / mRNA splicing, via spliceosome / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / single-stranded RNA binding / nuclear body / nuclear speck / mRNA binding / enzyme binding / protein homodimerization activity / RNA binding / zinc ion binding / extracellular exosome / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
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Method | ![]() ![]() | ||||||
![]() | Pomeranz Krummel, D.A. / Oubridge, C. / Leung, A.K. / Li, J. / Nagai, K. | ||||||
![]() | ![]() Title: Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Authors: Pomeranz Krummel, D.A. / Oubridge, C. / Leung, A.K. / Li, J. / Nagai, K. #1: ![]() Title: Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Authors: Kambach, C. / Walke, S. / Young, R. / Avis, J.M. / de la Fortelle, E. / Raker, V.A. / Luhrmann, R. / Li, J. / Nagai, K. #2: ![]() Title: Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis Authors: Leung, A.K.W. / Nagai, K. / Li, J. #3: ![]() Title: The structure and biochemical properties of the human spliceosomal protein U1C. Authors: Muto, Y. / Pomeranz Krummel, D. / Oubridge, C. / Hernandez, H. / Robinson, C.V. / Neuhaus, D. / Nagai, K. #4: ![]() Title: A retroviral RNA kissing complex containing only two G.C base pairs. Authors: Kim, C.H. / Tinoco, I. #5: ![]() Title: Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Authors: Oubridge, C. / Ito, N. / Evans, P.R. / Teo, C.H. / Nagai, K. #6: Journal: Nucleic Acids Res. / Year: 1990 Title: Solution structure of human U1 snRNA. Derivation of a possible three-dimensional model. Authors: Krol, A. / Westhof, E. / Bach, M. / Luhrmann, R. / Ebel, J.P. / Carbon, P. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 144.3 KB | Display | ![]() |
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PDB format | ![]() | 75.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480 KB | Display | ![]() |
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Full document | ![]() | 480 KB | Display | |
Data in XML | ![]() | 1.7 KB | Display | |
Data in CIF | ![]() | 31 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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Unit cell |
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Components
-Small nuclear ribonucleoprotein ... , 6 types, 24 molecules DSTUBMNOCPQRFZ12EWXYG345
#2: Protein | Mass: 13956.373 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #4: Protein | Mass: 13310.653 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #5: Protein | Mass: 13551.928 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #6: Protein | Mass: 9734.171 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: Coexpressed with Sm E and Sm G, entities 6 and 7 Gene: SNRPF, PBSCF / Plasmid: pET15b / Production host: ![]() ![]() #7: Protein | Mass: 10817.601 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: Coexpressed with Sm F and Sm G, entities 5 and 7 Gene: SNRPE / Plasmid: pET15b / Production host: ![]() ![]() #8: Protein | Mass: 8508.084 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: Coexpressed with Sm F and Sm E, entities 5 and 6 Gene: SNRPG, PBSCG / Plasmid: pET15b / Production host: ![]() ![]() |
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-U1 small nuclear ribonucleoprotein ... , 2 types, 8 molecules K678L90l
#9: Protein | Mass: 25372.779 Da / Num. of mol.: 4 / Fragment: residues 1-215 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #10: Protein | Mass: 8800.039 Da / Num. of mol.: 4 / Fragment: residues 1-77 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-RNA chain / Protein / Non-polymers , 3 types, 12 molecules VvwxAHIJ![](data/chem/img/ZN.gif)
![](data/chem/img/ZN.gif)
#11: Chemical | ChemComp-ZN / #1: RNA chain | Mass: 44418.223 Da / Num. of mol.: 4 Fragment: Nucleotides 57-82 absent, replaced with kissing loop Mutation: C53G,G54A,A55G,G56A,U83C,A85U Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #3: Protein | Mass: 18003.979 Da / Num. of mol.: 4 / Fragment: residues 1-174 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.92 % | ||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.6 Details: 38-40% MPD, 0.3M KCl, 0.1M MES.KOH, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||
Components of the solutions |
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-Data collection
Diffraction |
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Radiation |
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Radiation wavelength |
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Reflection | Redundancy: 7.9 % / Av σ(I) over netI: 3.8 / Number: 111105 / Rmerge(I) obs: 0.084 / Rsym value: 0.084 / D res high: 6.5 Å / D res low: 103.721 Å / Num. obs: 14148 / % possible obs: 96.9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 5.493→123.091 Å / Num. all: 28397 / Num. obs: 28397 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.9 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 12.9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Resolution: 5.493→5.78 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.691 / Mean I/σ(I) obs: 1.1 / Num. measured all: 31601 / Num. unique all: 4031 / % possible all: 98.3 |
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Processing
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Refinement | Resolution: 5.493→123.091 Å / Num. reflection all: 28397 / Num. reflection obs: 28397 / Isotropic thermal model: Isotropic / σ(F): 0 Details: Refinement not applicable with C-alpha & phosphorous atom only model | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 231.62 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 5.493→123.091 Å
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