Download MendeleyThe structure of a putative acetyltransferase from Listeria innocua.
Cuff, M.E., Tesar, C., Freeman, L., Joachimiak, A.To be published.
3FNC
Crystal structure of a putative acetyltransferase from Listeria innocua
- PDB DOI: https://doi.org/10.2210/pdb3FNC/pdb
- Classification: TRANSFERASE
- Organism(s): Listeria innocua Clip11262
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-12-24 Released: 2009-01-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.75 Å
- R-Value Free: 0.201
- R-Value Work: 0.169
- R-Value Observed: 0.170
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 |
| Putative acetyltransferase | 163 | Listeria innocua Clip11262 | Mutation(s): 0 Gene Names: lin0611 |  | |
UniProt | |||||
Find proteins for Q92E50 (Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)) Explore Q92E50 Go to UniProtKB: Q92E50 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q92E50 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MLI Query on MLI | C [auth A], D [auth A], L [auth B] | MALONATE ION C3 H2 O4 OFOBLEOULBTSOW-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | E [auth A] F [auth A] G [auth A] H [auth A] I [auth A] | 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: 1.75 Å
- R-Value Free: 0.201
- R-Value Work: 0.169
- R-Value Observed: 0.170
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.974 | α = 90 |
| b = 61.03 | β = 92.08 |
| c = 75.132 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| MLPHARE | phasing |
| DM | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| SOLVE | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
| CCP4 | phasing |
| O | model building |
| Coot | model building |
Entry History
Deposition Data
- Released Date: 2009-01-27 Deposition Author(s): Cuff, M.E., Tesar, C., Freeman, L., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-01-27
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description
