SUMO activating enzyme complex / SUMO activating enzyme activity / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / ubiquitin activating enzyme activity / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) ...SUMO activating enzyme complex / SUMO activating enzyme activity / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / ubiquitin activating enzyme activity / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / PML body organization / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of action potential / small protein activating enzyme binding / positive regulation of protein sumoylation / SUMO binding / regulation of calcium ion transmembrane transport / SUMOylation of DNA methylation proteins / SUMOylation of immune response proteins / XY body / SUMOylation of SUMOylation proteins / ATP-dependent protein binding / Maturation of nucleoprotein / SUMOylation of RNA binding proteins / regulation of cardiac muscle cell contraction / Transferases; Acyltransferases; Aminoacyltransferases / ubiquitin-like protein conjugating enzyme binding / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / positive regulation of protein targeting to mitochondrion / negative regulation of protein import into nucleus / SUMOylation of ubiquitinylation proteins / roof of mouth development / ubiquitin-specific protease binding / negative regulation of DNA binding / ubiquitin-like protein ligase binding / transcription factor binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation / potassium channel regulator activity / SUMOylation of DNA damage response and repair proteins / nuclear pore / Regulation of IFNG signaling / enzyme activator activity / cellular response to cadmium ion / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / SUMOylation of intracellular receptors / positive regulation of protein-containing complex assembly / PKR-mediated signaling / negative regulation of DNA-binding transcription factor activity / PML body / Formation of Incision Complex in GG-NER / protein tag activity / regulation of protein localization / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to heat / transferase activity / nuclear membrane / nuclear body / protein stabilization / nuclear speck / protein heterodimerization activity / DNA repair / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / nucleolus / enzyme binding / magnesium ion binding / RNA binding / nucleoplasm / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 215 / Source method: isolated from a natural source / Formula: H2O
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Details
Nonpolymer details
THE CYS-GLY-GLY-AVSN LIGAND, WHERE AVSN HAS ID VMX IN THIS FILE, WAS LINKED TO SUMO1 BY INTEIN- ...THE CYS-GLY-GLY-AVSN LIGAND, WHERE AVSN HAS ID VMX IN THIS FILE, WAS LINKED TO SUMO1 BY INTEIN-MEDIATED LIGATION. THERE IS A CROSS-LINK BETWEEN ATOM SG IN RESIDUE CYS 173 B AND C10 IN LIGAND VMX 97 D
Sequence details
CHAIN D IS COMPOSED AS UB/UBI-CYS-GLY-GLY-AVSN.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 2
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Sample preparation
Crystal
Density Matthews: 2.36 Å3/Da / Density % sol: 47.83 %
Crystal grow
Temperature: 279 K / Method: vapor diffusion, hanging drop Details: 22% PEG 2000 MME, 0.2 M di-ammonium tartrate, 3% EtGly, VAPOR DIFFUSION, HANGING DROP, temperature 279K
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Data collection
Diffraction
ID
Mean temperature (K)
Crystal-ID
1
100
1
2
1
1,2
1
Diffraction source
Source
Site
Beamline
ID
Wavelength (Å)
SYNCHROTRON
APS
24-ID-C
1
0.979
SYNCHROTRON
APS
24-ID-C
2
0.979
Detector
Type
ID
Detector
Date
ADSC QUANTUM 315
1
CCD
Oct 27, 2008
ADSC QUANTUM 315
2
CCD
Nov 9, 2008
Radiation
ID
Protocol
Monochromatic (M) / Laue (L)
Scattering type
Wavelength-ID
1
SINGLEWAVELENGTH
M
x-ray
1
2
SINGLEWAVELENGTH
M
x-ray
1
Radiation wavelength
Wavelength: 0.979 Å / Relative weight: 1
Reflection
Resolution: 2.6→25 Å / Num. obs: 33019 / % possible obs: 99 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.074 / Net I/σ(I): 15.8
Reflection shell
Resolution: 2.6→2.67 Å / Rmerge(I) obs: 0.367 / Mean I/σ(I) obs: 2.7 / % possible all: 96.1
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