3b78

Structure of the eEF2-ExoA(R551H)-NAD+ complex

Method: X-RAY DIFFRACTION Dmax: 197.0 Å Quality: REASONABLE

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

Elongation factor 2

OrganismNot specified

UniProt P32324

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 1–842 Non-standard monomer:Yes (specific site not provided by mmCIF) Exotoxin A × 1 (P11439) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–842 Non-standard monomer:Yes (specific site not provided by mmCIF) Exotoxin A × 1 (P11439) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–842 Non-standard monomer:Yes (specific site not provided by mmCIF) Exotoxin A × 1 (P11439) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242

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.

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

View Construct and Data Evidence
UniProt name EF2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–842; UniProt 1–842 Author chain C; PDBConstruct 1–842; UniProt 1–842 Author chain E; PDBConstruct 1–842; UniProt 1–842

Exotoxin A

Pseudomonas aeruginosa

UniProt P11439

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 425–630 Fragment:catalytic domain Mutation:R551H Elongation factor 2 × 1 (P32324) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 425–630 Fragment:catalytic domain Mutation:R551H Elongation factor 2 × 1 (P32324) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 425–630 Fragment:catalytic domain Mutation:R551H Elongation factor 2 × 1 (P32324) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;293 K;7% PEG-10000, 3.5mM MPD, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.242

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOXA_PSEAE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–207; UniProt 425–630 Author chain D; PDBConstruct 2–207; UniProt 425–630 Author chain F; PDBConstruct 2–207; UniProt 425–630

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 3b78

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3b78
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3b78
Deposition date deposition_date2007-10-30
Structure title titleStructure of the eEF2-ExoA(R551H)-NAD+ complex
Keywords keywords;elongation factor, toxin, ADP-ribosylation, toxin-substrate complex, Cytoplasm, GTP-binding, Nucleotide-binding, Phosphoprotein, Protein biosynthesis, RNA-binding, rRNA-binding, Glycosyltransferase, NAD, Transferase, BIOSYNTHETIC PROTEIN-TRANSFERASE COMPLEX ;; BIOSYNTHETIC PROTEIN/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier64.13
Radius of gyration Rg (electron density) rg_electron64.69
Forward intensity I(0) i01634730000.00
Molecular weight molecular_weight342470.0 kDa
Excluded volume excluded_volume430130 ų
Envelope volume envelope_volume668800 ų
Hydration-shell volume shell_volume91695 ų
Envelope diameter envelope_diameter212.2
Shell Rg shell_rg58.30
Envelope Rg envelope_rg62.61
Shape Rg shape_rg64.71
Total Rg total_rg64.48
Total atoms total_atoms24118
Residues n_residues3087
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 dmax197.0
Rg (real space) rg_real64.49
Rg uncertainty (real space) rg_real_error1.96
I(0) (real space) i0_real1.6350e+09
I(0) uncertainty (real space) i0_real_error3.5370e+07
Rg (reciprocal space) rg_reciprocal63.76
I(0) (reciprocal space) i0_reciprocal1633000000.0000
Solution quality estimate total_estimate0.6057
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.9
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40390000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 0.999; Sysdev: 0.013; Positv: 1.000; Valcen: 0.992; Smooth: 0.016

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 42 domains

SCOP 2.08 (21 domains)

Domain ID domain_idd3b78a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3b78a2
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.3 — Translation proteins
Family Family familyb.43.3.1 — Elongation factors
Domain ID domain_idd3b78a3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78a4
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.1 — Translational machinery components
Domain ID domain_idd3b78a5
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78b1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.166 — ADP-ribosylation
Superfamily Superfamily superfamilyd.166.1 — ADP-ribosylation
Family Family familyd.166.1.1 — ADP-ribosylating toxins
Domain ID domain_idd3b78b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3b78c1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3b78c2
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.3 — Translation proteins
Family Family familyb.43.3.1 — Elongation factors
Domain ID domain_idd3b78c3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78c4
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.1 — Translational machinery components
Domain ID domain_idd3b78c5
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78d1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.166 — ADP-ribosylation
Superfamily Superfamily superfamilyd.166.1 — ADP-ribosylation
Family Family familyd.166.1.1 — ADP-ribosylating toxins
Domain ID domain_idd3b78d2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3b78e1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3b78e2
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.3 — Translation proteins
Family Family familyb.43.3.1 — Elongation factors
Domain ID domain_idd3b78e3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78e4
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.1 — Translational machinery components
Domain ID domain_idd3b78e5
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.11 — EF-G C-terminal domain-like
Family Family familyd.58.11.1 — EF-G/eEF-2 domains III and V
Domain ID domain_idd3b78f1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.166 — ADP-ribosylation
Superfamily Superfamily superfamilyd.166.1 — ADP-ribosylation
Family Family familyd.166.1.1 — ADP-ribosylating toxins
Domain ID domain_idd3b78f2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (21 domains)

Domain ID domain_id3b78A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3b78A02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1430 — Yeast translation eEF2 (G' domain)
Homologous superfamily homologous superfamily10 — Yeast translation eEF2 (G' domain)
Domain ID domain_id3b78A03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id3b78A04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily870 — Elongation Factor G (Translational Gtpase), domain 3
Domain ID domain_id3b78A05
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id3b78A06
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily240
Domain ID domain_id3b78B00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology175 — Diphtheria Toxin; domain 1
Homologous superfamily homologous superfamily10 — Diphtheria Toxin, domain 1
Domain ID domain_id3b78C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3b78C02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1430 — Yeast translation eEF2 (G' domain)
Homologous superfamily homologous superfamily10 — Yeast translation eEF2 (G' domain)
Domain ID domain_id3b78C03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id3b78C04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily870 — Elongation Factor G (Translational Gtpase), domain 3
Domain ID domain_id3b78C05
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id3b78C06
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily240
Domain ID domain_id3b78D00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology175 — Diphtheria Toxin; domain 1
Homologous superfamily homologous superfamily10 — Diphtheria Toxin, domain 1
Domain ID domain_id3b78E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3b78E02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1430 — Yeast translation eEF2 (G' domain)
Homologous superfamily homologous superfamily10 — Yeast translation eEF2 (G' domain)
Domain ID domain_id3b78E03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id3b78E04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily870 — Elongation Factor G (Translational Gtpase), domain 3
Domain ID domain_id3b78E05
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id3b78E06
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily240
Domain ID domain_id3b78F00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology175 — Diphtheria Toxin; domain 1
Homologous superfamily homologous superfamily10 — Diphtheria Toxin, domain 1

8. Citations (1)

9. Files and Curves (10)