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- PDB-2n7d: Solution structure of the UBL domain of human Ddi2 -

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Basic information

Entry
Database: PDB / ID: 2n7d
TitleSolution structure of the UBL domain of human Ddi2
ComponentsProtein DDI1 homolog 2
KeywordsUNKNOWN FUNCTION / DDI2
Function / homology
Function and homology information


regulation of DNA stability / cellular response to hydroxyurea / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / proteasomal protein catabolic process / ubiquitin binding / regulation of protein stability / protein processing / chromosome / aspartic-type endopeptidase activity / nucleoplasm ...regulation of DNA stability / cellular response to hydroxyurea / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / proteasomal protein catabolic process / ubiquitin binding / regulation of protein stability / protein processing / chromosome / aspartic-type endopeptidase activity / nucleoplasm / identical protein binding / cytosol
Similarity search - Function
DNA damage inducible protein 1 ubiquitin-like domain / Aspartic peptidase, DDI1-type / Aspartyl protease / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin domain profile. / Ubiquitin-like domain / Aspartic peptidase domain superfamily / Ubiquitin-like domain superfamily ...DNA damage inducible protein 1 ubiquitin-like domain / Aspartic peptidase, DDI1-type / Aspartyl protease / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin domain profile. / Ubiquitin-like domain / Aspartic peptidase domain superfamily / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Protein DDI1 homolog 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics, molecular dynamics
AuthorsSiva, M. / Grantz Saskova, K. / Veverka, V.
CitationJournal: Sci Rep / Year: 2016
Title: Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog.
Authors: Siva, M. / Svoboda, M. / Veverka, V. / Trempe, J.F. / Hofmann, K. / Kozisek, M. / Hexnerova, R. / Sedlak, F. / Belza, J. / Brynda, J. / Sacha, P. / Hubalek, M. / Starkova, J. / Flaisigova, I. ...Authors: Siva, M. / Svoboda, M. / Veverka, V. / Trempe, J.F. / Hofmann, K. / Kozisek, M. / Hexnerova, R. / Sedlak, F. / Belza, J. / Brynda, J. / Sacha, P. / Hubalek, M. / Starkova, J. / Flaisigova, I. / Konvalinka, J. / Saskova, K.G.
History
DepositionSep 8, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jul 20, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 3, 2016Group: Database references
Revision 1.2Aug 10, 2016Group: Structure summary
Revision 1.3Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein DDI1 homolog 2


Theoretical massNumber of molelcules
Total (without water)11,1421
Polymers11,1421
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)40 / 100structures with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein Protein DDI1 homolog 2


Mass: 11142.463 Da / Num. of mol.: 1 / Fragment: UBL domain (UNP residues 1-76)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DDI2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5TDH0

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D HN(CA)CB
1313D CBCA(CO)NH
1413D (H)CCH-TOCSY
1513D 1H-13C NOESY
1613D 1H-15N NOESY
1713D HNCO

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Sample preparation

DetailsContents: 25 mM sodium phosphate, 100 mM sodium chloride, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
25 mMsodium phosphate-11
100 mMsodium chloride-21
Sample conditionsIonic strength: 0.1 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE8501
Bruker AvanceBrukerAVANCE6002

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Processing

NMR software
NameDeveloperClassification
YASARAYASARArefinement
CYANAGuntert, Mumenthaler and Wuthrichrefinement
RefinementMethod: torsion angle dynamics, molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 40

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