Download MendeleyCrystal structure of T4 gp33 bound to E. coli RNAP beta-flap domain
Twist, K.A.F., Campbell, E.A., Darst, S.A., Geiduschek, E.P., Hochschild, A., Deighan, P.To be published.
3TBI
Crystal structure of T4 gp33 bound to E. coli RNAP beta-flap domain
- PDB DOI: https://doi.org/10.2210/pdb3TBI/pdb
- Classification: TRANSCRIPTION
- Organism(s): Tequatrovirus T4, Escherichia coli
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2011-08-06 Released: 2011-11-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.295
- R-Value Work: 0.251
- R-Value Observed: 0.253
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| RNA polymerase-associated protein Gp33 | 115 | Tequatrovirus T4 | Mutation(s): 0 Gene Names: 33, gp33 |  | |
UniProt | |||||
Find proteins for P13338 (Enterobacteria phage T4) Explore P13338 Go to UniProtKB: P13338 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P13338 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| DNA-directed RNA polymerase subunit beta | 228 | Escherichia coli | Mutation(s): 0 Gene Names: b3987, groN, JW3950, nitB, rif, ron, rpoB, stl, stv, tabD EC: 2.7.7.6 |  | |
UniProt | |||||
Find proteins for P0A8V2 (Escherichia coli (strain K12)) Explore P0A8V2 Go to UniProtKB: P0A8V2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0A8V2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.295
- R-Value Work: 0.251
- R-Value Observed: 0.253
- Space Group: I 2 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 55.218 | α = 90 |
| b = 112.25 | β = 90 |
| c = 164.847 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| SnB | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| SCALA | data scaling |
Entry History
Deposition Data
- Released Date: 2011-11-23 Deposition Author(s): Twist, K.A.F., Campbell, E.A., Darst, S.A.
Revision History (Full details and data files)
- Version 1.0: 2011-11-23
Type: Initial release
