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- PDB-5d1k: Crystal Structure of UbcH5B in Complex with the RING-U5BR Fragmen... -

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Basic information

Entry
Database: PDB / ID: 5d1k
TitleCrystal Structure of UbcH5B in Complex with the RING-U5BR Fragment of AO7
Components
  • E3 ubiquitin-protein ligase RNF25
  • Ubiquitin-conjugating enzyme E2 D2
KeywordsLIGASE / ubiquitin conjugating enzyme (E2) / ubiquitin ligase (E3) / RING finger / ubiquitination / ubiquitin
Function / homology
Function and homology information


(E3-independent) E2 ubiquitin-conjugating enzyme / protein K6-linked ubiquitination / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / NF-kappaB binding / protein autoubiquitination / protein K48-linked ubiquitination / cytosolic ribosome / ubiquitin ligase complex / rescue of stalled ribosome ...(E3-independent) E2 ubiquitin-conjugating enzyme / protein K6-linked ubiquitination / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / NF-kappaB binding / protein autoubiquitination / protein K48-linked ubiquitination / cytosolic ribosome / ubiquitin ligase complex / rescue of stalled ribosome / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / Negative regulators of DDX58/IFIH1 signaling / Peroxisomal protein import / Regulation of TNFR1 signaling / RING-type E3 ubiquitin transferase / protein modification process / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / CLEC7A (Dectin-1) signaling / FCERI mediated NF-kB activation / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / E3 ubiquitin ligases ubiquitinate target proteins / Neddylation / positive regulation of NF-kappaB transcription factor activity / ubiquitin-dependent protein catabolic process / protein ubiquitination / ubiquitin protein ligase binding / protein-containing complex / extracellular exosome / nucleoplasm / ATP binding / nucleus / metal ion binding / cytosol
Similarity search - Function
E3 ubiquitin-protein ligase RNF25 / RWD domain / RWD domain / RWD domain profile. / RWD / Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. ...E3 ubiquitin-protein ligase RNF25 / RWD domain / RWD domain / RWD domain profile. / RWD / Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Ubiquitin-conjugating enzyme/RWD-like / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
OXALATE ION / DI(HYDROXYETHYL)ETHER / Ubiquitin-conjugating enzyme E2 D2 / E3 ubiquitin-protein ligase RNF25
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.78 Å
AuthorsLiang, Y.-H. / Li, S. / Weissman, A.M. / Ji, X.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.
Authors: Li, S. / Liang, Y.H. / Mariano, J. / Metzger, M.B. / Stringer, D.K. / Hristova, V.A. / Li, J. / Randazzo, P.A. / Tsai, Y.C. / Ji, X. / Weissman, A.M.
History
DepositionAug 4, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 28, 2015Provider: repository / Type: Initial release
Revision 1.1Dec 30, 2015Group: Database references
Revision 1.2Aug 30, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: audit_author / chem_comp_atom ...audit_author / chem_comp_atom / chem_comp_bond / citation / citation_author / database_2 / pdbx_struct_oper_list / struct_keywords
Item: _audit_author.identifier_ORCID / _citation.journal_id_CSD ..._audit_author.identifier_ORCID / _citation.journal_id_CSD / _citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _struct_keywords.pdbx_keywords
Revision 1.3Sep 27, 2023Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 D2
B: E3 ubiquitin-protein ligase RNF25
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,8649
Polymers32,3532
Non-polymers5117
Water4,540252
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3370 Å2
ΔGint-8 kcal/mol
Surface area14950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.470, 45.658, 67.954
Angle α, β, γ (deg.)90.000, 118.090, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-334-

HOH

21A-353-

HOH

31A-367-

HOH

41A-453-

HOH

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein Ubiquitin-conjugating enzyme E2 D2 / Ubiquitin carrier protein D2 / Ubiquitin-conjugating enzyme E2(17)KB 2 / Ubiquitin-conjugating ...Ubiquitin carrier protein D2 / Ubiquitin-conjugating enzyme E2(17)KB 2 / Ubiquitin-conjugating enzyme E2-17 kDa 2 / Ubiquitin-protein ligase D2 / p53-regulated ubiquitin-conjugating enzyme 1


Mass: 16755.227 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B / Plasmid: pETDUET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P62837, ubiquitin-protein ligase
#2: Protein E3 ubiquitin-protein ligase RNF25 / RING finger protein 25


Mass: 15597.544 Da / Num. of mol.: 1 / Fragment: UNP residues 126-258
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RNF25 / Plasmid: pETDUET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3)
References: UniProt: Q96BH1, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)

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Non-polymers , 5 types, 259 molecules

#3: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical ChemComp-OXL / OXALATE ION


Mass: 88.019 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2O4
#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 252 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.23 Å3/Da / Density % sol: 44.86 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 20% PEG-10000, 8% ethylene glycol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Nov 18, 2009 / Details: mirrors
RadiationMonochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.78→50 Å / Num. all: 27616 / Num. obs: 27367 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Biso Wilson estimate: 23.52 Å2 / Rmerge(I) obs: 0.057 / Χ2: 1.037 / Net I/σ(I): 11.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allΧ2% possible all
1.78-1.845.60.4673.01325331.01692.7
1.84-1.926.30.3674.48827210.94398.7
1.92-26.90.277.51327371.077100
2-2.117.10.19510.78427461.103100
2.11-2.247.20.14713.88227301.031100
2.24-2.427.20.11717.32927620.993100
2.42-2.667.30.0923.22627351.041100
2.66-3.047.30.06231.9327790.982100
3.04-3.837.40.03656.63627811.075100
3.83-507.30.02869.12428431.09399.9

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Processing

Software
NameVersionClassification
HKL-3000data reduction
PHENIX1.7.3_928refinement
PDB_EXTRACT3.11data extraction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2ESK

2esk


Resolution: 1.78→33.339 Å / Occupancy max: 1 / Occupancy min: 0.27 / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.76 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.202 896 3.28 %RANDOM
Rwork0.1696 ---
obs0.1707 27356 99.14 %-
all-27593 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.517 Å2 / ksol: 0.346 e/Å3
Displacement parametersBiso max: 109.11 Å2 / Biso mean: 29.4482 Å2 / Biso min: 12.12 Å2
Baniso -1Baniso -2Baniso -3
1--2.9938 Å20 Å2-0.2222 Å2
2--6.6062 Å2-0 Å2
3----3.6124 Å2
Refinement stepCycle: LAST / Resolution: 1.78→33.339 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2070 0 27 252 2349
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072296
X-RAY DIFFRACTIONf_angle_d1.0863137
X-RAY DIFFRACTIONf_chiral_restr0.073327
X-RAY DIFFRACTIONf_plane_restr0.005417
X-RAY DIFFRACTIONf_dihedral_angle_d13.337927
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection allNum. reflection obs% reflection obs (%)
1.78-1.89150.31241420.286341764318431895
1.8915-2.03760.26051490.1856442145704570100
2.0376-2.24260.20771500.1652442145714571100
2.2426-2.5670.20881490.1711443345824582100
2.567-3.23370.20321520.1683445846104610100
3.2337-33.34490.17171540.154455147054705100

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