SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation ...SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation / SUMOylation of DNA damage response and repair proteins / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / SUMOylation of intracellular receptors / PML body / Formation of Incision Complex in GG-NER / protein tag activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Processing of DNA double-strand break ends / ubiquitin protein ligase binding / RNA binding / nucleoplasm / nucleus Similarity search - Function
THE PROTEIN CHAIN IS SEGMENTED INTO DIFFERENT ASUS VIA A CRYSTALLOGRAPHIC SYMMETRY AXIS. THUS THE DIMERIC ASSEMBLY IS ACTUALLY A MONOMER IN WHICH THE HALVES ARE RELATED BY SYMMETRY AND LINKED VIA AN UNOBSERVED LINKER
Mass: 19185.377 Da / Num. of mol.: 1 / Fragment: SUMO-2DELTAN11, RESIDUES 12-93 Source method: isolated from a genetically manipulated source Details: LINEAR FUSION-PROTEIN OF 2 SUMO2-DELTAN11 FRAGMENTS, WHICH ARE PRESENT IN DIFFERENT ASU, RELATED VIA A CRYSTALLOGRAPHIC SYMMETRY AXIS Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-4T2 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P61956
Resolution: 2.11→19.76 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.918 / SU B: 5.426 / SU ML: 0.14 / Cross valid method: THROUGHOUT / ESU R: 0.287 / ESU R Free: 0.208 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 17-89 MAKE UP THE CONTENT OF THE ASU. RESIDUES 101-173 ARE IDENTICAL TO RESIDUES 17-89, AND SEGMENTED INTO DIFFERENT ASU VIA A ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 17-89 MAKE UP THE CONTENT OF THE ASU. RESIDUES 101-173 ARE IDENTICAL TO RESIDUES 17-89, AND SEGMENTED INTO DIFFERENT ASU VIA A CRYSTALLOGRAPHIC SYMMETRY AXIS. THE GAP OF APPROX. 14 A BETWEEN THE C-TERMINUS OF A MOLECULE IN A ASU TO THE N-TERMINUS OF A SYMMETRY-RELATED MOLECULE IN THE ADJACENT ASU CAN BE FILLED BY 11 RESIDUES FROM THE LINKER (90-100) WHICH ARE DELOCALIZED. THE TERMINAL RESIDUES 10-16 AND 174-177 ARE FLEXIBLE AND NOT OBSERVED IN THE CRYSTAL STRUCTURE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.23074
171
4.5 %
RANDOM
Rwork
0.17872
-
-
-
obs
0.18092
3668
94.79 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK