2mbq

K11-linked Diubiquitin average solution structure at pH 6.8, 150 mM NaCl

Method: SOLUTION NMR Dmax: 63.7 Å Quality: REASONABLE

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

Ubiquitin

Homo sapiens

UniProt P0CG48

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–76 Chain B; UniProt 1–76 Fragment:UNP residues 1-76 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;296 K;Ionic strength (raw mmCIF value) 150;Pressure ambient NMR sample composition:75 uM [U-99% 15N] ubiquitin, 20 mM sodium phosphate, 150 mM sodium chloride, 93% H2O/7% D2O | 93% H2O/7% 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76

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 2mbq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mbq
Deposition date deposition_date2013-08-03
Structure title titleK11-linked Diubiquitin average solution structure at pH 6.8, 150 mM NaCl
Keywords keywordsdiubiquitin, K11, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.63
Radius of gyration Rg (electron density) rg_electron18.71
Forward intensity I(0) i04911950.00
Molecular weight molecular_weight16327.0 kDa
Excluded volume excluded_volume20662 ų
Envelope volume envelope_volume25322 ų
Hydration-shell volume shell_volume12549 ų
Envelope diameter envelope_diameter63.6
Shell Rg shell_rg22.87
Envelope Rg envelope_rg18.67
Shape Rg shape_rg18.70
Total Rg total_rg19.51
Total atoms total_atoms2346
Residues n_residues144
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 dmax63.7
Rg (real space) rg_real19.78
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real4.9120e+06
I(0) uncertainty (real space) i0_real_error6.4050e+04
Rg (reciprocal space) rg_reciprocal19.76
I(0) (reciprocal space) i0_reciprocal4912000.0000
Solution quality estimate total_estimate0.7484
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.457
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3228000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.637; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.819; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2mbqa_
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
Domain ID domain_idd2mbqb_
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 (2 domains)

Domain ID domain_id2mbqA00
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
Domain ID domain_id2mbqB00
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)