Download MendeleyHigh resolution crystal structure of transketolase from Campylobacter jejuni subsp. jejuni NCTC 11168
Nocek, B., Makowska-Grzysa, M., Maltseva, N., Grimshaw, S., Anderson, W.F., Joachimiak, A.To be published.
3L84
High resolution crystal structure of transketolase from Campylobacter jejuni subsp. jejuni NCTC 11168
- PDB DOI: https://doi.org/10.2210/pdb3L84/pdb
- Classification: TRANSFERASE
- Organism(s): Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2009-12-29 Released: 2010-02-09
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.36 Å
- R-Value Free: 0.152
- R-Value Work: 0.132
- R-Value Observed: 0.133
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 |
| Transketolase | 632 | Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819 | Mutation(s): 0 Gene Names: tkt, Cj1645 EC: 2.2.1.1 |  | |
UniProt | |||||
Find proteins for Q0P7Y3 (Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)) Explore Q0P7Y3 Go to UniProtKB: Q0P7Y3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q0P7Y3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | B [auth A], C [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | D [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| 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: 1.36 Å
- R-Value Free: 0.152
- R-Value Work: 0.132
- R-Value Observed: 0.133
- Space Group: C 1 2 1
- Diffraction Data: https://doi.org/10.18430/M33L84
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 129.493 | α = 90 |
| b = 71.181 | β = 109.77 |
| c = 69.416 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | phasing |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2010-02-09 Deposition Author(s): Nocek, B., Makowska-Grzyska, M., Maltseva, N., Grimshaw, S., Anderson, W., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2010-02-09
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2012-02-22
Changes: Structure summary
