Download MendeleyKirromycin Defines a Specific Domain Arrangement of Elongation Factor EF-TU
Nielsen, R.C., Kristensen, O., Kjeldgaard, M., Thirup, S., Nissen, P.To be published.
1OB2
E. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNA
- PDB DOI: https://doi.org/10.2210/pdb1OB2/pdb
- NAKB: 1OB2
- Classification: HYDROLASE/NUCLEAR PROTEIN
- Organism(s): Escherichia coli BL21, Saccharomyces cerevisiae
- Mutation(s): No
- Deposited: 2003-01-24 Released: 2004-05-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.35 Å
- R-Value Free: 0.265
- R-Value Work: 0.220
- R-Value Observed: 0.220
This is version 2.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| ELONGATION FACTOR TU | 393 | Escherichia coli BL21 | Mutation(s): 0 EC: 3.6.1.48 |  | |
UniProt | |||||
Find proteins for P0CE48 (Escherichia coli (strain K12)) Explore P0CE48 Go to UniProtKB: P0CE48 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0CE48 | ||||
Sequence AnnotationsExpand | |||||
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Find similar nucleic acids by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | Organism | Image | |
| TRANSFER-RNA, PHE | 77 | Saccharomyces cerevisiae |  | ||
Sequence AnnotationsExpand | |||||
| |||||
Oligosaccharides
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| KIR Query on KIR | D [auth A] | KIRROMYCIN C43 H60 N2 O12 HMSYAPGFKGSXAJ-PAHGNTJYSA-N |  | ||
| GNP Query on GNP | E [auth A] | PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER C10 H17 N6 O13 P3 UQABYHGXWYXDTK-UUOKFMHZSA-N |  | ||
| MG Query on MG | F [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| PHA Query on PHA | B | L-PEPTIDE LINKING | C9 H11 N O |  | PHE |
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
| PRD_900003 Query on PRD_900003 | C | sucrose | Oligosaccharide / Nutrient |  | |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.35 Å
- R-Value Free: 0.265
- R-Value Work: 0.220
- R-Value Observed: 0.220
- Space Group: P 41 3 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 196.41 | α = 90 |
| b = 196.41 | β = 90 |
| c = 196.41 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| DENZO | data reduction |
| Agrovata | data scaling |
| AMoRE | phasing |
Entry History
Deposition Data
- Released Date: 2004-05-27 Deposition Author(s): Kristensen, O., Nissen, P., Nyborg, J.
Revision History (Full details and data files)
- Version 1.0: 2004-05-27
Type: Initial release - Version 1.1: 2012-11-14
Changes: Database references, Derived calculations, Non-polymer description, Other, Refinement description, Structure summary, Version format compliance - Version 1.2: 2015-08-19
Changes: Atomic model, Derived calculations, Non-polymer description, Other, Structure summary - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Non-polymer description, Other, Structure summary - Version 2.1: 2023-12-13
Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary
