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1efc

INTACT ELONGATION FACTOR FROM E.COLI

Method: X-RAY DIFFRACTION Dmax: 107.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (ELONGATION FACTOR)

Escherichia coli

UniProt P0A6N1

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 2–394 Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5 Resolution 2.05 Å R-free 0.268
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 2–394 Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5 Resolution 2.05 Å R-free 0.268

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 1EFC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1D8T CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC Deposited 1999-10-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–393（393 aa）
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACT ACETATE ION × 19 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6；TRIS-HCL, MAGNESIUM CHLORIDE, GDP, POLYETHYLENE GLYCOL 3350, AMMONIUM ACETATE, AMMONIUM CITRATE, PH 7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.K
Resolution 2.35 Å R-free 0.246
1D8T CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC Deposited 1999-10-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACT ACETATE ION × 11 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6；TRIS-HCL, MAGNESIUM CHLORIDE, GDP, POLYETHYLENE GLYCOL 3350, AMMONIUM ACETATE, AMMONIUM CITRATE, PH 7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.K
Resolution 2.35 Å R-free 0.246
1DG1 WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU). Deposited 1999-11-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain G 1–394（394 aa）
Chain H 1–394（394 aa）
Not recorded MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.75；298 K；PEG 3350, ammonium citrate, ammonium acetate, pH 5.75, VAPOR DIFFUSION, temperature 298.0K
Resolution 2.50 Å R-free 0.259
1EFU ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI Deposited 1996-07-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 9–393（385 aa）
Chain C 9–393（385 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；pH 7.7
Resolution 2.50 Å R-free 0.283
1ETU STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY Deposited 1988-01-15 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–392（392 aa）
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.90 Å
1LS2 Fitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome Deposited 2002-05-16 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric
Chain A 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer Hepes-KOH buffer at pH 7.5；pH 7.5；Hepes-KOH buffer at pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Rapid-freezing in liquid ethane
Resolution 16.80 Å
1QZD EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome Deposited 2003-09-16 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer Polymix buffer；pH 7.5；Polymix buffer
cryo-EM vitrification conditions Cryogen ETHANE；Rapid-freezing in liquid ethane
Resolution 10.00 Å
2BVN E. coli EF-Tu:GDPNP in complex with the antibiotic enacyloxin IIa Deposited 2005-06-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–393（393 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ENX ENACYLOXIN IIA × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；292 K；2 MICROL PROTEIN SOLUTION MIXED WITH 1 MICROL RESERVOIR SOLUTION (450 MM NACL. 22% PEG6000, 6% GLYCEROL, 7 MM MGCL2, 100 MM TRIS-HCL PH 7.5), SITTING DROP 19 DEG. C
Resolution 2.30 Å R-free 0.271
2BVN E. coli EF-Tu:GDPNP in complex with the antibiotic enacyloxin IIa Deposited 2005-06-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–393（393 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ENX ENACYLOXIN IIA × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；292 K；2 MICROL PROTEIN SOLUTION MIXED WITH 1 MICROL RESERVOIR SOLUTION (450 MM NACL. 22% PEG6000, 6% GLYCEROL, 7 MM MGCL2, 100 MM TRIS-HCL PH 7.5), SITTING DROP 19 DEG. C
Resolution 2.30 Å R-free 0.271
2HCJ Trypsin-modified Elongation Factor Tu in complex with tetracycline Deposited 2006-06-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain B 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 NA SODIUM ION × 3 TAC TETRACYCLINE × 1 GLV GLYOXYLIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；VAPOR DIFFUSION, SITTING DROP
Resolution 2.12 Å R-free 0.234
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain B 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 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 C 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain D 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain F 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain G 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain H 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain I 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain J 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain K 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain L 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TAC TETRACYCLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain B 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Chain C 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain D 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TAC TETRACYCLINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain J 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Chain K 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain L 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TAC TETRACYCLINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution Deposited 2006-06-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 9 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain F 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Chain G 8–44（37 aa） Fragment：EF-Tu fragment, residues 8-44
Chain H 59–393（335 aa） Fragment：EF-Tu fragment, residues 59-393
Not recorded MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TAC TETRACYCLINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP
Resolution 2.80 Å R-free 0.223
3EP2 Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM Deposited 2008-09-29 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: nonameric
Chain X 2–394（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å
3EQ3 Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM Deposited 2008-09-30 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: nonameric
Chain X 2–394（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；HiFi buffer (50 mM Tris-HCl pH 7.5, 70mM NH4Cl, 30 mM KCl, 3.5 mM MgCl2, 0.5 mM spermidine, 8mM putrescine, 2 mM DTT, 3.5 mM MgCl2)
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 9.00 Å
3EQ4 Model of tRNA(Leu)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM Deposited 2008-09-30 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: nonameric
Chain X 2–394（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.3；Polymix buffer( 5 mM potassium phosphate (KH2PO4) pH 7.3, 5 mM NH4Cl, 95 mM KCl, 0.5 mM CaCl2, 8 mM putrescine, 1 mM spermidine, 1 mM DTE, 5 mM magnesium acetate)
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 12.00 Å
4V69 Ternary complex-bound E.coli 70S ribosome. Deposited 2008-12-11 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 51 PDB declaration: 58-meric
Chain AZ 2–394（393 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Vitrification using FEI Vitrobot; blot 3 seconds before plunging with an offset of -1mm
Resolution 6.70 Å

13 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFTU_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–393； UniProt 2–394 Author chain B； PDBConstruct 1–393； UniProt 2–394

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 1efc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1efc
Deposition date deposition_date1998-11-24
Structure title titleINTACT ELONGATION FACTOR FROM E.COLI
Keywords keywordsTRANSPORT AND PROTECTION PROTEIN, RNA BINDING PROTEIN; RNA BINDING PROTEIN
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_guinier33.88 Å
Radius of gyration Rg (electron density) rg_electron33.37 Å
Forward intensity I(0) i0116087000.00
Molecular weight molecular_weight85396.0 kDa
Excluded volume excluded_volume106760 ų
Envelope volume envelope_volume139960 ų
Hydration-shell volume shell_volume34809 ų
Envelope diameter envelope_diameter110.9 Å
Shell Rg shell_rg40.02 Å
Envelope Rg envelope_rg32.81 Å
Shape Rg shape_rg33.33 Å
Total Rg total_rg34.03 Å
Total atoms total_atoms5998
Residues n_residues772
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 dmax107.7 Å
Rg (real space) rg_real33.86 Å
Rg uncertainty (real space) rg_real_error0.86 Å
I(0) (real space) i0_real1.1610e+08
I(0) uncertainty (real space) i0_real_error1.9110e+06
Rg (reciprocal space) rg_reciprocal33.88 Å
I(0) (reciprocal space) i0_reciprocal116100000.0000
Solution quality estimate total_estimate0.8931
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary— Å
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.2350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16220000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.804
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1efca1
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_idd1efca2
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_idd1efca3
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_idd1efcb1
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_idd1efcb2
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_idd1efcb3
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

CATH v4.4 (6 domains)

Domain ID domain_id1efcA01
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_id1efcA02
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_id1efcA03
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_id1efcB01
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_id1efcB02
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_id1efcB03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
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8. Citations (6)

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9. Files and Curves (10)