4oyj

Structure of the apo HOIP PUB domain

Method: X-RAY DIFFRACTION Dmax: 135.0 Å Quality: GOOD

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

E3 ubiquitin-protein ligase RNF31

Homo sapiens

UniProt Q96EP0

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 1–184 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
10 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain J; UniProt 1–184 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
11 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain K; UniProt 1–184 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
12 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain L; UniProt 1–184 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
13 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain M; UniProt 1–184 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–184 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–184 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–184 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 1–184 Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 1–184 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 1–184 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 1–184 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 1–184 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;295 K;1.3 M ammonium sulphate, 200 mM KI, 100 mM Tris, pH 8.5 Resolution 3.00 Å R-free 0.255

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.

35 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNF31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–186; UniProt 1–184 Author chain B; PDBConstruct 3–186; UniProt 1–184 Author chain C; PDBConstruct 3–186; UniProt 1–184 Author chain D; PDBConstruct 3–186; UniProt 1–184 Author chain E; PDBConstruct 3–186; UniProt 1–184 Author chain F; PDBConstruct 3–186; UniProt 1–184 Author chain G; PDBConstruct 3–186; UniProt 1–184 Author chain H; PDBConstruct 3–186; UniProt 1–184 Author chain I; PDBConstruct 3–186; UniProt 1–184 Author chain J; PDBConstruct 3–186; UniProt 1–184 Author chain K; PDBConstruct 3–186; UniProt 1–184 Author chain L; PDBConstruct 3–186; UniProt 1–184 Author chain M; PDBConstruct 3–186; UniProt 1–184

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 4oyj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4oyj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4oyj
Deposition date deposition_date2014-02-12
Structure title titleStructure of the apo HOIP PUB domain
Keywords keywordsE3 ubiquitin ligase, PUB domain, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.13
Radius of gyration Rg (electron density) rg_electron43.45
Forward intensity I(0) i01055530000.00
Molecular weight molecular_weight260890.0 kDa
Excluded volume excluded_volume324030 ų
Envelope volume envelope_volume463950 ų
Hydration-shell volume shell_volume86148 ų
Envelope diameter envelope_diameter137.7
Shell Rg shell_rg51.06
Envelope Rg envelope_rg42.24
Shape Rg shape_rg43.46
Total Rg total_rg43.75
Total atoms total_atoms18383
Residues n_residues2333
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 dmax135.0
Rg (real space) rg_real43.84
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.0560e+09
I(0) uncertainty (real space) i0_real_error1.6990e+07
Rg (reciprocal space) rg_reciprocal44.13
I(0) (reciprocal space) i0_reciprocal1056000000.0000
Solution quality estimate total_estimate0.8924
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.2
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.535
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113000000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 13 domains

CATH v4.4 (13 domains)

Domain ID domain_id4oyjA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjF00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjG00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjH00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjI00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjJ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjK00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjL00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190
Domain ID domain_id4oyjM00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2190

8. Citations (1)

9. Files and Curves (10)