5jg6

APC11-Ubv shows role of noncovalent RING-Ubiquitin interactions in processive multiubiquitination and Ubiquitin chain elongation by APC/C

Method: X-RAY DIFFRACTION Dmax: 93.2 Å Quality: GOOD

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

Anaphase-promoting complex subunit 11

Homo sapiens

UniProt Q9NYG5

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 17–84 Not recorded Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Ammonium acetate, 0.1 M Sodium acetate pH 4.6, 33% PEG4000 Resolution 2.00 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 17–84 Not recorded Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Ammonium acetate, 0.1 M Sodium acetate pH 4.6, 33% PEG4000 Resolution 2.00 Å R-free 0.220

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.

22 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APC11_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–70; UniProt 17–84 Author chain D; PDBConstruct 3–70; UniProt 17–84

Polyubiquitin-B

Homo sapiens

UniProt P0CG47

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 76–154 Not recorded Anaphase-promoting complex subunit 11 × 1 (Q9NYG5) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Ammonium acetate, 0.1 M Sodium acetate pH 4.6, 33% PEG4000 Resolution 2.00 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 76–154 Not recorded Anaphase-promoting complex subunit 11 × 1 (Q9NYG5) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Ammonium acetate, 0.1 M Sodium acetate pH 4.6, 33% PEG4000 Resolution 2.00 Å R-free 0.220

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.

278 other PDB entries and 428 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–84; UniProt 76–154 Author chain C; PDBConstruct 6–84; UniProt 76–154

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 5jg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jg6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5jg6
Deposition date deposition_date2016-04-19
Structure title titleAPC11-Ubv shows role of noncovalent RING-Ubiquitin interactions in processive multiubiquitination and Ubiquitin chain elongation by APC/C
Keywords keywordsRING Ubiquitin Cell Cycle Anaphase-promoting complex-Cyclosome, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.87
Radius of gyration Rg (electron density) rg_electron26.12
Forward intensity I(0) i018451400.00
Molecular weight molecular_weight31185.0 kDa
Excluded volume excluded_volume38300 ų
Envelope volume envelope_volume49090 ų
Hydration-shell volume shell_volume17578 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg29.91
Envelope Rg envelope_rg25.98
Shape Rg shape_rg25.99
Total Rg total_rg26.95
Total atoms total_atoms2150
Residues n_residues279
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 dmax93.2
Rg (real space) rg_real27.23
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.8450e+07
I(0) uncertainty (real space) i0_real_error2.8680e+05
Rg (reciprocal space) rg_reciprocal27.13
I(0) (reciprocal space) i0_reciprocal18450000.0000
Solution quality estimate total_estimate0.7877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1633000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.330; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5jg6b1
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.15.1.0 — automated matches
Domain ID domain_idd5jg6b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5jg6c_
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.15.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id5jg6A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id5jg6D00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)