Download MendeleyThe structure of a putative ModE from Agrobacterium tumefaciens.
Cuff, M.E., Evdokimova, E., Kudritska, M., Edwards, A., Savchenko, A., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)To be published.
2IJL
The structure of a putative ModE from Agrobacterium tumefaciens.
- PDB DOI: https://doi.org/10.2210/pdb2IJL/pdb
- Classification: TRANSCRIPTION
- Organism(s): Agrobacterium fabrum str. C58
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2006-09-29 Released: 2006-10-31
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.236
- R-Value Work: 0.174
- R-Value Observed: 0.177
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Molybdenum-binding transcriptional repressor | 135 | Agrobacterium fabrum str. C58 | Mutation(s): 7 Gene Names: modE |  | |
UniProt | |||||
Find proteins for A9CHN1 (Agrobacterium fabrum (strain C58 / ATCC 33970)) Explore A9CHN1 Go to UniProtKB: A9CHN1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A9CHN1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | C [auth A] D [auth A] E [auth A] F [auth A] I [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | G [auth A] H [auth A] M [auth B] N [auth B] O [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.236
- R-Value Work: 0.174
- R-Value Observed: 0.177
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 40.719 | α = 90 |
| b = 79.536 | β = 106.7 |
| c = 43.994 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| HKL-3000 | phasing |
| SHELX | phasing |
| MLPHARE | phasing |
| DM | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
| O | model building |
| Coot | model building |
Entry History
Deposition Data
- Released Date: 2006-10-31 Deposition Author(s): Cuff, M.E., Evdokimova, E., Kudritska, M., Edwards, A., Savchenko, A., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-10-31
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance
