2awt

Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)

Method: SOLUTION NMR Dmax: 38.6 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Small ubiquitin-related modifier 2

Homo sapiens

UniProt P61956

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–95 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;303 K;Ionic strength (raw mmCIF value) 50mM sodium phosphate, 150mM NaCl;Pressure ambient NMR sample composition:0.8mM SUMO-2 U-15N, 13C; 50mM phosphate buffer pH 6.0; 150mM NaCl; 1mM EDTA; 1mM DSS; 0.01% sodium azide; 90% H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

24 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUMO2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–95; UniProt 1–95

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2awt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2awt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2awt
Deposition date deposition_date2005-09-02
Structure title titleSolution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)
Keywords keywordsubiquitin fold, half-open barrel, two helices, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.29
Radius of gyration Rg (electron density) rg_electron14.73
Forward intensity I(0) i0732910000.00
Molecular weight molecular_weight217020.0 kDa
Excluded volume excluded_volume267310 ų
Envelope volume envelope_volume55649 ų
Hydration-shell volume shell_volume22577 ų
Envelope diameter envelope_diameter86.1
Shell Rg shell_rg27.51
Envelope Rg envelope_rg22.14
Shape Rg shape_rg14.67
Total Rg total_rg15.26
Total atoms total_atoms30080
Residues n_residues1900
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax38.6
Rg (real space) rg_real14.41
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real6.9620e+08
I(0) uncertainty (real space) i0_real_error5.2530e+06
Rg (reciprocal space) rg_reciprocal15.36
I(0) (reciprocal space) i0_reciprocal732900000.0000
Solution quality estimate total_estimate0.6879
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.7680
Highest regularization parameter α highest_alpha466100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.019; Oscil: 0.999; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2awta_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

CATH v4.4 (1 domains)

Domain ID domain_id2awtA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)