5H07

TNIP2-Ub complex, C2 form

> Summary

Summary for 5H07

DescriptorPolyubiquitin-C, TNFAIP3-interacting protein 2
Functional Keywordscoiled-coil, complex, signal transduction, signaling protein
Biological sourceHomo sapiens (Human)
Cellular locationUbiquitin: Cytoplasm  P0CG48
Cytoplasm  Q8NFZ5
Total number of polymer chains3
Total molecular weight47128.51
Authors
Lo, Y.C.,Lin, S.C. (deposition date: 2016-10-04, release date: 2017-03-08)
Primary citation
Lin, S.M.,Lin, S.C.,Hong, J.Y.,Su, T.W.,Kuo, B.J.,Chang, W.H.,Tu, Y.F.,Lo, Y.C.
Structural Insights into Linear Tri-ubiquitin Recognition by A20-Binding Inhibitor of NF-kappa B, ABIN-2
Structure, 25:66-78, 2017
PubMed: 27916521
DOI: 10.1016/j.str.2016.11.005
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.586 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.272901.5%9.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 5h07
no rotation
Molmil generated image of 5h07
rotated about x axis by 90°
Molmil generated image of 5h07
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
APolyubiquitin-Cpolymer22825694.51
UniProt (P0CG48)
Pfam (PF00240)
Homo sapiens (Human)
D, CTNFAIP3-interacting protein 2polymer9110717.02
UniProt (Q8NFZ5)
Pfam (PF16516)
Homo sapiens (Human)A20-binding inhibitor of NF-kappa-B activation 2,ABIN-2,Fetal liver LKB1-interacting protein
waterwater18.098

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains3
Total molecular weight47128.5
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight47128.5
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.586 Å)

Cell axes98.76580.97265.352
Cell angles90.00114.2890.00
SpacegroupC 1 2 1
Resolution limits19.86 - 2.59
the highest resolution shell value2.689 - 2.586
R-factor0.2177
R-work0.21130
the highest resolution shell value0.230
R-free0.27340
the highest resolution shell value0.283
RMSD bond length0.002
RMSD bond angle0.517

Data Collection Statistics

Resolution limits30.00 - 2.59
the highest resolution shell value -
Number of reflections12803
Completeness99.2
Redundancy3.5

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP298

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI12Activating enzyme.
ChainResidueDetails
AARG54
AARG72

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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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