2den

Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin

Method: SOLUTION NMR Dmax: 51.3 Å Quality: REASONABLE

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

Immunoglobulin G-binding protein G,Ubiquitin-like protein 7

Homo sapiens

UniProt P06654

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 229–282 Fragment:UBA domain,UBA domain Mutation:I12A Polyubiquitin-B × 1 (J3QS39) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:1mM HGB1-UBA | 20mM phosphate, 100mM NaCl, pH6.5 NMR sample composition:1mM Ubiquitin | 20mM phosphate, 100mM NaCl, pH6.5 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.

48 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG1_STRSG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–62; UniProt 229–282

Immunoglobulin G-binding protein G,Ubiquitin-like protein 7

Homo sapiens

UniProt Q96S82

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 336–380 Fragment:UBA domain,UBA domain Mutation:I12A Polyubiquitin-B × 1 (J3QS39) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:1mM HGB1-UBA | 20mM phosphate, 100mM NaCl, pH6.5 NMR sample composition:1mM Ubiquitin | 20mM phosphate, 100mM NaCl, pH6.5 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBL7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 64–108; UniProt 336–380

Polyubiquitin-B

Homo sapiens

UniProt J3QS39

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–76 Not recorded Immunoglobulin G-binding protein G,Ubiquitin-like protein 7 × 1 (P06654,Q96S82) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:1mM HGB1-UBA | 20mM phosphate, 100mM NaCl, pH6.5 NMR sample composition:1mM Ubiquitin | 20mM phosphate, 100mM NaCl, pH6.5 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.

38 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name J3QS39_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges 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 2den

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2den
Deposition date deposition_date2006-02-14
Structure title titleSolution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin
Keywords keywordsA:alpha-alpha-alpha, B:beta-beta-helix-helix-beta-beta-helix-beta, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.26
Radius of gyration Rg (electron density) rg_electron14.75
Forward intensity I(0) i0259672000.00
Molecular weight molecular_weight134690.0 kDa
Excluded volume excluded_volume168700 ų
Envelope volume envelope_volume26085 ų
Hydration-shell volume shell_volume14172 ų
Envelope diameter envelope_diameter54.3
Shell Rg shell_rg21.44
Envelope Rg envelope_rg16.08
Shape Rg shape_rg14.75
Total Rg total_rg14.93
Total atoms total_atoms19120
Residues n_residues1220
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 dmax51.3
Rg (real space) rg_real15.75
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real2.5870e+08
I(0) uncertainty (real space) i0_real_error2.5300e+06
Rg (reciprocal space) rg_reciprocal15.25
I(0) (reciprocal space) i0_reciprocal259700000.0000
Solution quality estimate total_estimate0.6469
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.9
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.165
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha7.7960
Highest regularization parameter α highest_alpha492800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 0.907; Sysdev: 0.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.464

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2dena_
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.2 — UBA-like
Family Family familya.5.2.0 — automated matches
Domain ID domain_idd2denb_
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_id2denA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id2denB00
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)