3tmp

The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde

Method: X-RAY DIFFRACTION Dmax: 102.3 Å Quality: EXCELLENT

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

OTU domain-containing protein 5

Homo sapiens

UniProt Q96G74

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 172–351 Fragment:catalytic or OTU domain (Residues 172-351) Mutation:S172 phosphorylated Non-standard monomer:Yes (specific site not provided by mmCIF) Polyubiquitin-C × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 172–351 Fragment:catalytic or OTU domain (Residues 172-351) Mutation:S172 phosphorylated Non-standard monomer:Yes (specific site not provided by mmCIF) Polyubiquitin-C × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 172–351 Fragment:catalytic or OTU domain (Residues 172-351) Mutation:S172 phosphorylated Non-standard monomer:Yes (specific site not provided by mmCIF) Polyubiquitin-C × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 172–351 Fragment:catalytic or OTU domain (Residues 172-351) Mutation:S172 phosphorylated Non-standard monomer:Yes (specific site not provided by mmCIF) Polyubiquitin-C × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OTUD5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–184; UniProt 172–351 Author chain C; PDBConstruct 5–184; UniProt 172–351 Author chain E; PDBConstruct 5–184; UniProt 172–351 Author chain G; PDBConstruct 5–184; UniProt 172–351

Polyubiquitin-C

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–76 Fragment:Ubiquitin-like 1 Non-standard monomer:Yes (specific site not provided by mmCIF) OTU domain-containing protein 5 × 1 (Q96G74) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–76 Fragment:Ubiquitin-like 1 Non-standard monomer:Yes (specific site not provided by mmCIF) OTU domain-containing protein 5 × 1 (Q96G74) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–76 Fragment:Ubiquitin-like 1 Non-standard monomer:Yes (specific site not provided by mmCIF) OTU domain-containing protein 5 × 1 (Q96G74) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–76 Fragment:Ubiquitin-like 1 Non-standard monomer:Yes (specific site not provided by mmCIF) OTU domain-containing protein 5 × 1 (Q96G74) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.91 Å R-free 0.227

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 345 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain F; PDBConstruct 1–76; UniProt 1–76 Author chain H; 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 3tmp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3tmp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3tmp
Deposition date deposition_date2011-08-31
Structure title titleThe catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde
Keywords keywordsOTU fold, Deubiquitinase, phosphorylation, Hydrolase-Protein Binding complex; Hydrolase/Protein Binding
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.99
Radius of gyration Rg (electron density) rg_electron32.09
Forward intensity I(0) i0211524000.00
Molecular weight molecular_weight111380.0 kDa
Excluded volume excluded_volume137390 ų
Envelope volume envelope_volume179260 ų
Hydration-shell volume shell_volume46214 ų
Envelope diameter envelope_diameter110.6
Shell Rg shell_rg39.35
Envelope Rg envelope_rg31.60
Shape Rg shape_rg32.09
Total Rg total_rg32.68
Total atoms total_atoms7820
Residues n_residues953
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 dmax102.3
Rg (real space) rg_real32.79
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real2.1150e+08
I(0) uncertainty (real space) i0_real_error2.9710e+06
Rg (reciprocal space) rg_reciprocal32.88
I(0) (reciprocal space) i0_reciprocal211500000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.8
Skewness Skewness skewness0.142
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32610000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3tmpb_
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_idd3tmpd_
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_idd3tmpf_
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_idd3tmph_
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 (8 domains)

Domain ID domain_id3tmpA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily80
Domain ID domain_id3tmpB00
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_id3tmpC01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily80
Domain ID domain_id3tmpD00
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_id3tmpE01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily80
Domain ID domain_id3tmpF00
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_id3tmpG01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily80
Domain ID domain_id3tmpH00
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)