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- PDB-4a0k: STRUCTURE OF DDB1-DDB2-CUL4A-RBX1 BOUND TO A 12 BP ABASIC SITE CO... -
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Basic information
Entry | Database: PDB / ID: 4a0k | ||||||
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Title | STRUCTURE OF DDB1-DDB2-CUL4A-RBX1 BOUND TO A 12 BP ABASIC SITE CONTAINING DNA-DUPLEX | ||||||
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![]() | LIGASE/DNA-BINDING PROTEIN/DNA / LIGASE-DNA-BINDING PROTEIN-DNA COMPLEX / DNA-BINDING PROTEIN-DNA COMPLEX | ||||||
Function / homology | ![]() Dual Incision in GG-NER / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Neddylation / Prolactin receptor signaling / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual Incision in GG-NER ...Dual Incision in GG-NER / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Neddylation / Prolactin receptor signaling / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual Incision in GG-NER / Dual incision in TC-NER / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Regulation of RAS by GAPs / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of DVL / Orc1 removal from chromatin / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Hedgehog 'on' state / negative regulation of granulocyte differentiation / Degradation of beta-catenin by the destruction complex / eukaryotic initiation factor 4E binding / Interleukin-1 signaling / KEAP1-NFE2L2 pathway / anaphase-promoting complex / GLI3 is processed to GLI3R by the proteasome / cullin-RING-type E3 NEDD8 transferase / Neddylation / cullin-RING ubiquitin ligase complex / Antigen processing: Ubiquitination & Proteasome degradation / regulation of DNA damage checkpoint / positive regulation by virus of viral protein levels in host cell / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / regulation of nucleotide-excision repair / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / VCB complex / positive regulation of protein autoubiquitination / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / protein neddylation / NEDD8 ligase activity / Cul5-RING ubiquitin ligase complex / biological process involved in interaction with symbiont / negative regulation of response to oxidative stress / regulation of mitotic cell cycle phase transition / ubiquitin-ubiquitin ligase activity / Cul4A-RING E3 ubiquitin ligase complex / SCF ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / negative regulation of type I interferon production / WD40-repeat domain binding / ubiquitin ligase complex scaffold activity / Cul4B-RING E3 ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / Cul3-RING ubiquitin ligase complex / negative regulation of reproductive process / negative regulation of developmental process / protein monoubiquitination / site of DNA damage / cullin family protein binding / somatic stem cell population maintenance / hemopoiesis / viral release from host cell / ectopic germ cell programmed cell death / proteasomal protein catabolic process / positive regulation of G1/S transition of mitotic cell cycle / protein K48-linked ubiquitination / positive regulation of viral genome replication / response to UV / ubiquitin ligase complex / positive regulation of gluconeogenesis / positive regulation of TORC1 signaling / T cell activation / intrinsic apoptotic signaling pathway / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / cellular response to amino acid stimulus / DNA Damage Recognition in GG-NER / RING-type E3 ubiquitin transferase / protein catabolic process / regulation of circadian rhythm / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Dual Incision in GG-NER / Wnt signaling pathway / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / G1/S transition of mitotic cell cycle / positive regulation of protein catabolic process / ubiquitin-protein transferase activity / cellular response to UV / ubiquitin protein ligase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / rhythmic process Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() SYNTHETIC CONSTRUCT (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fischer, E.S. / Scrima, A. / Gut, H. / Thoma, N.H. | ||||||
![]() | ![]() Title: The Molecular Basis of Crl4(Ddb2/Csa) Ubiquitin Ligase Architecture, Targeting, and Activation. Authors: Fischer, E.S. / Scrima, A. / Bohm, K. / Matsumoto, S. / Lingaraju, G.M. / Faty, M. / Yasuda, T. / Cavadini, S. / Wakasugi, M. / Hanaoka, F. / Iwai, S. / Gut, H. / Sugasawa, K. / Thoma, N.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 942 KB | Display | ![]() |
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PDB format | ![]() | 772.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4a08C ![]() 4a09C ![]() 4a0aC ![]() 4a0bC ![]() 4a0cC ![]() 4a0lC ![]() 4a11C ![]() 2hyeS ![]() 3ei2S C: citing same article ( S: Starting model for refinement |
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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
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 86702.836 Da / Num. of mol.: 1 / Fragment: RESIDUES 38-759 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 13626.354 Da / Num. of mol.: 1 / Fragment: RESIDUES 12-108 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P62878, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) |
-DNA DAMAGE-BINDING PROTEIN ... , 2 types, 2 molecules CD
#3: Protein | Mass: 129394.898 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#4: Protein | Mass: 43418.102 Da / Num. of mol.: 1 / Fragment: RESIDUES 60-423 Source method: isolated from a genetically manipulated source Details: VARIANT WITH GLN AT POSITION 180 AND ARG AT POSITION 214 (SIMILAR TO PDB ENTRY 3EI2) Source: (gene. exp.) ![]() ![]() ![]() |
-DNA chain , 2 types, 2 molecules EF
#5: DNA chain | Mass: 3498.283 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
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#6: DNA chain | Mass: 3702.428 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.8 Å3/Da / Density % sol: 68 % / Description: NONE |
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Crystal grow | pH: 8.3 / Details: 100MM TRIS-HCL PH 8.3, 33% PEG 200 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 30, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 5.93→50 Å / Num. obs: 11289 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Redundancy: 4.9 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 5.93→6.08 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.41 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 2HYE AND 3EI2 Resolution: 5.93→19.977 Å / SU ML: 0.91 / σ(F): 2.05 / Phase error: 30.59 / Stereochemistry target values: ML Details: THE MOLECULAR REPLACEMENT SOLUTION HAS BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED RESOLUTION. RBX1 RESIDUES 40-108 ...Details: THE MOLECULAR REPLACEMENT SOLUTION HAS BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED RESOLUTION. RBX1 RESIDUES 40-108 HAVE BEEN REMOVED DUE TO UNCERTAINTY OF CONFORMATIONS. STEREOCHEMISTRY IS BASED ON THE SEARCH MODELS 3EI2 AND 2HYE.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 236.778 Å2 / ksol: 0.314 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 299 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 5.93→19.977 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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