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1aip

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Method: X-RAY DIFFRACTION Dmax: 197.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ELONGATION FACTOR TU

Thermus thermophilus

UniProt P60338

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–405 Chain B； UniProt 1–405 Not recorded ELONGATION FACTOR TS × 2 （P43895） X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000 Resolution 3.00 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain E； UniProt 1–405 Chain F； UniProt 1–405 Not recorded ELONGATION FACTOR TS × 2 （P43895） X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000 Resolution 3.00 Å R-free 0.289

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.

Other PDB Difference from Current Entry 1AIP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EXM CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS ELONGATION FACTOR TU (EF-TU) IN COMPLEX WITH THE GTP ANALOGUE GPPNHP. Deposited 2000-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–406（405 aa） Fragment：INTACT WILD-TYPE EF-TU
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；20mM Sodium cacodylate, 5mM Magnesium sulfate, 38-44% Ammonium sulfate, 7-10 mg/mL EF-Tu, molar ratio EF-Tu:GppNHp = 1:5, pH 7.0, VAPOR DIFFUSION, HANGING DROP
Resolution 1.70 Å R-free 0.243
4H9G Probing EF-Tu with a very small brominated fragment library identifies the CCA pocket Deposited 2012-09-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–406（405 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 8 14J 5-bromofuran-2-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M tris, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.93 Å R-free 0.184
4LBV Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.03 Å R-free 0.193
4LBV Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 CL CHLORIDE ION × 2 SO4 SULFATE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.03 Å R-free 0.193
4LBW Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.74 Å R-free 0.194
4LBW Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.74 Å R-free 0.194
4LBY Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.69 Å R-free 0.207
4LBZ Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.212
4LBZ Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.212
4LC0 Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.201
4LC0 Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–406（404 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；292 K；1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.201

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFTU1_THETH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–405； UniProt 1–405 Author chain B； PDBConstruct 1–405； UniProt 1–405 Author chain E； PDBConstruct 1–405； UniProt 1–405 Author chain F； PDBConstruct 1–405； UniProt 1–405

ELONGATION FACTOR TS

Thermus thermophilus

UniProt P43895

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain C； UniProt 1–196 Chain D； UniProt 1–196 Not recorded ELONGATION FACTOR TU × 2 （P60338） X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000 Resolution 3.00 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain G； UniProt 1–196 Chain H； UniProt 1–196 Not recorded ELONGATION FACTOR TU × 2 （P60338） X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000 Resolution 3.00 Å R-free 0.289

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.

Other PDB Difference from Current Entry 1AIP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1TFE DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS Deposited 1996-04-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 55–196（142 aa） Fragment：EF-TS DIMERIZATION DOMAIN, RESIDUES 55 - 196
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å R-free 0.285

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFTS_THET8
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 1–196； UniProt 1–196 Author chain D； PDBConstruct 1–196； UniProt 1–196 Author chain G； PDBConstruct 1–196； UniProt 1–196 Author chain H； PDBConstruct 1–196； UniProt 1–196

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 1aip

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aip
Deposition date deposition_date1997-04-22
Structure title titleEF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS
Keywords keywordsELONGATION FACTOR, NUCLEOTIDE EXCHANGE, GTP-BINDING, COMPLEX OF TWO ELONGATION FACTORS; COMPLEX OF TWO ELONGATION FACTORS
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier58.26 Å
Radius of gyration Rg (electron density) rg_electron58.72 Å
Forward intensity I(0) i0901729000.00
Molecular weight molecular_weight249760.0 kDa
Excluded volume excluded_volume312700 ų
Envelope volume envelope_volume481880 ų
Hydration-shell volume shell_volume73238 ų
Envelope diameter envelope_diameter214.0 Å
Shell Rg shell_rg54.36 Å
Envelope Rg envelope_rg57.28 Å
Shape Rg shape_rg58.72 Å
Total Rg total_rg58.60 Å
Total atoms total_atoms17560
Residues n_residues2269
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax197.5 Å
Rg (real space) rg_real58.71 Å
Rg uncertainty (real space) rg_real_error1.71 Å
I(0) (real space) i0_real9.0170e+08
I(0) uncertainty (real space) i0_real_error1.8450e+07
Rg (reciprocal space) rg_reciprocal57.86 Å
I(0) (reciprocal space) i0_reciprocal900500000.0000
Solution quality estimate total_estimate0.8419
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.5 Å
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.1350 Å−1
Current regularization parameter α current_alpha0.0008
Highest regularization parameter α highest_alpha39340000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.391
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 44 domains

SCOP 2.08 (20 domains)

Domain ID domain_idd1aipa1
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_idd1aipa2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1aipa3
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_idd1aipb1
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_idd1aipb2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1aipb3
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_idd1aipc1
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.2 — UBA-like
Family Family familya.5.2.2 — TS-N domain
Domain ID domain_idd1aipc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.43 — EF-Ts domain-like
Superfamily Superfamily superfamilyd.43.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Family Family familyd.43.1.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Domain ID domain_idd1aipd1
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.2 — UBA-like
Family Family familya.5.2.2 — TS-N domain
Domain ID domain_idd1aipd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.43 — EF-Ts domain-like
Superfamily Superfamily superfamilyd.43.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Family Family familyd.43.1.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Domain ID domain_idd1aipe1
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_idd1aipe2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1aipe3
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_idd1aipf1
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_idd1aipf2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1aipf3
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_idd1aipg1
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.2 — UBA-like
Family Family familya.5.2.2 — TS-N domain
Domain ID domain_idd1aipg2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.43 — EF-Ts domain-like
Superfamily Superfamily superfamilyd.43.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Family Family familyd.43.1.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Domain ID domain_idd1aiph1
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.2 — UBA-like
Family Family familya.5.2.2 — TS-N domain
Domain ID domain_idd1aiph2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.43 — EF-Ts domain-like
Superfamily Superfamily superfamilyd.43.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Family Family familyd.43.1.1 — Elongation factor Ts (EF-Ts), dimerisation domain

CATH v4.4 (24 domains)

Domain ID domain_id1aipA01
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_id1aipA02
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_id1aipA03
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_id1aipB01
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_id1aipB02
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_id1aipB03
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_id1aipC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology479 — Tetrahydropterin Synthase; Chain A
Homologous superfamily homologous superfamily20 — Elongation factor Ts, dimerisation domain
Domain ID domain_id1aipC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1aipC03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id1aipD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology479 — Tetrahydropterin Synthase; Chain A
Homologous superfamily homologous superfamily20 — Elongation factor Ts, dimerisation domain
Domain ID domain_id1aipD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1aipD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id1aipE01
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_id1aipE02
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_id1aipE03
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_id1aipF01
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_id1aipF02
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_id1aipF03
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_id1aipG01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology479 — Tetrahydropterin Synthase; Chain A
Homologous superfamily homologous superfamily20 — Elongation factor Ts, dimerisation domain
Domain ID domain_id1aipG02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1aipG03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id1aipH01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology479 — Tetrahydropterin Synthase; Chain A
Homologous superfamily homologous superfamily20 — Elongation factor Ts, dimerisation domain
Domain ID domain_id1aipH02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1aipH03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
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8. Citations (1)

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9. Files and Curves (10)