Download MendeleyThe C-terminal part of BipA protein from Vibrio parahaemolyticus RIMD 2210633
Nocek, B., Mulligan, R., Duggan, E., Clancy, S., Joachimiak, A.To be published.
3E3X
The C-terminal part of BipA protein from Vibrio parahaemolyticus RIMD 2210633
- PDB DOI: https://doi.org/10.2210/pdb3E3X/pdb
- Classification: HYDROLASE
- Organism(s): Vibrio parahaemolyticus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-08-08 Released: 2008-09-30
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.223
- R-Value Work: 0.172
- R-Value Observed: 0.174
wwPDB Validation 3D Report Full Report
This is version 1.1 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 |
| BipA | 332 | Vibrio parahaemolyticus | Mutation(s): 0 Gene Names: bipA, VP0122 |  | |
UniProt | |||||
Find proteins for Q9L5X8 (Vibrio parahaemolyticus) Explore Q9L5X8 Go to UniProtKB: Q9L5X8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9L5X8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | D [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | B [auth A], C [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MLY Query on MLY | A | L-PEPTIDE LINKING | C8 H18 N2 O2 |  | LYS |
| MLZ Query on MLZ | A | L-PEPTIDE LINKING | C7 H16 N2 O2 |  | LYS |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.223
- R-Value Work: 0.172
- R-Value Observed: 0.174
- Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 90.6 | α = 90 |
| b = 104.571 | β = 90 |
| c = 74.348 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELX | phasing |
| ARP | model building |
| Coot | model building |
| MLPHARE | phasing |
| CCP4 | phasing |
Entry History
Deposition Data
- Released Date: 2008-09-30 Deposition Author(s): Nocek, B., Mulligan, R., Duggan, E., Clancy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-09-30
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance
