5ulk

Crystal Structure of RNF165 in complex with a UbcH5b~Ub conjugate

Method: X-RAY DIFFRACTION Dmax: 80.2 Å Quality: GOOD

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

Ubiquitin-conjugating enzyme E2 D2

Homo sapiens

UniProt P62837

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–147 Mutation:C21S, C85K, C107S, C111S Ubiquitin × 1 (P0CG47) E3 ubiquitin-protein ligase RNF165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;200 mM ammonium nitrate, 20% PEG 3350 Resolution 2.38 Å R-free 0.267

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.

57 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–152; UniProt 1–147

Ubiquitin

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) E3 ubiquitin-protein ligase RNF165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;200 mM ammonium nitrate, 20% PEG 3350 Resolution 2.38 Å R-free 0.267

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 429 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 1–76; UniProt 1–76

E3 ubiquitin-protein ligase RNF165

Homo sapiens

UniProt Q6ZSG1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 255–346 Fragment:residues 292-340 Mutation:M313A Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) Ubiquitin × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;200 mM ammonium nitrate, 20% PEG 3350 Resolution 2.38 Å R-free 0.267

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN165_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–92; UniProt 255–346

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 5ulk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ulk
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5ulk
Deposition date deposition_date2017-01-24
Structure title titleCrystal Structure of RNF165 in complex with a UbcH5b~Ub conjugate
Keywords keywordsOpen conformation, Backside, Isopeptide-linked, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.91
Radius of gyration Rg (electron density) rg_electron23.16
Forward intensity I(0) i016477400.00
Molecular weight molecular_weight30938.0 kDa
Excluded volume excluded_volume38819 ų
Envelope volume envelope_volume47026 ų
Hydration-shell volume shell_volume18003 ų
Envelope diameter envelope_diameter82.4
Shell Rg shell_rg28.43
Envelope Rg envelope_rg23.12
Shape Rg shape_rg23.11
Total Rg total_rg24.01
Total atoms total_atoms2166
Residues n_residues270
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 dmax80.2
Rg (real space) rg_real24.00
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.6480e+07
I(0) uncertainty (real space) i0_real_error2.4600e+05
Rg (reciprocal space) rg_reciprocal23.98
I(0) (reciprocal space) i0_reciprocal16480000.0000
Solution quality estimate total_estimate0.8650
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.1
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4636000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5ulka_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5ulkb_
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_idd5ulkc_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5ulkC00
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)