1yd8

COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

Method: X-RAY DIFFRACTION Dmax: 102.2 Å Quality: SUSPICIOUS

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

UBIQUIN

OrganismNot specified

UniProt P62990

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 U; UniProt 1–76 Not recorded ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain V; UniProt 1–76 Not recorded ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.297

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.

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

View Construct and Data Evidence
UniProt name UBIQ_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain U; PDBConstruct 1–76; UniProt 1–76 Author chain V; PDBConstruct 1–76; UniProt 1–76

ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3

Homo sapiens

UniProt Q9NZ52

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 H; UniProt 208–301 Not recorded UBIQUIN × 1 (P62990) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 208–301 Not recorded UBIQUIN × 1 (P62990) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.297

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.

5 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GGA3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 5–98; UniProt 208–301 Author chain H; PDBConstruct 5–98; UniProt 208–301

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 1yd8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yd8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yd8
Deposition date deposition_date2004-12-23
Structure title titleCOMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
Keywords keywordsTRAFFICKING, POST TRANSLATIONAL MODIFICATION, MONO-UBIQUITINATION, PROTEIN TRANSPORT;, PROTEIN TRANSPORT, CHROMOSOMAL PROTEIN; PROTEIN TRANSPORT, CHROMOSOMAL PROTEIN
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_electron33.26
Forward intensity I(0) i024506400.00
Molecular weight molecular_weight37937.0 kDa
Excluded volume excluded_volume47254 ų
Envelope volume envelope_volume66738 ų
Hydration-shell volume shell_volume18712 ų
Envelope diameter envelope_diameter107.2
Shell Rg shell_rg35.84
Envelope Rg envelope_rg32.31
Shape Rg shape_rg33.27
Total Rg total_rg33.49
Total atoms total_atoms2662
Residues n_residues332
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 dmax102.2
Rg (real space) rg_real33.52
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.4510e+07
I(0) uncertainty (real space) i0_real_error3.9750e+05
Rg (reciprocal space) rg_reciprocal33.31
I(0) (reciprocal space) i0_reciprocal24500000.0000
Solution quality estimate total_estimate0.4858
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.846
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1604000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.607; Stabil: 0.998; Sysdev: 0.049; Positv: 1.000; Valcen: 0.327; Smooth: 0.021

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1yd8g1
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1yd8g2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1yd8h2
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1yd8h3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1yd8u_
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_idd1yd8v_
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 (4 domains)

Domain ID domain_id1yd8G00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1yd8H00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1yd8U00
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_id1yd8V00
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)