Download MendeleyCrystal structure of conserved domain protein from vibrio cholerae o1 biovar eltor str. n16961
Nocek, B., Duggan, E., Abdullah, J., Joachimiak, A.To be published.
3LKV
Crystal structure of conserved domain protein from vibrio cholerae o1 biovar eltor str. n16961
- PDB DOI: https://doi.org/10.2210/pdb3LKV/pdb
- Entry: 3LKV supersedes: 2QH8
- Classification: ATP binding protein
- Organism(s): Vibrio cholerae O1 biovar El Tor str. N16961
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2010-01-27 Released: 2010-03-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.203
- R-Value Work: 0.178
- R-Value Observed: 0.180
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 |
| uncharacterized CONSERVED DOMAIN PROTEIN | 302 | Vibrio cholerae O1 biovar El Tor str. N16961 | Mutation(s): 0 Gene Names: VC_1101 |  | |
UniProt | |||||
Find proteins for Q9KT04 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)) Explore Q9KT04 Go to UniProtKB: Q9KT04 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9KT04 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PHE Query on PHE | B [auth A] | PHENYLALANINE C9 H11 N O2 COLNVLDHVKWLRT-QMMMGPOBSA-N |  | ||
| SO4 Query on SO4 | F [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | G [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | C [auth A], D [auth A], E [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| 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: 2.20 ?
- R-Value Free: 0.203
- R-Value Work: 0.178
- R-Value Observed: 0.180
- Space Group: P 41 3 2
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 144.256 | ¦Á = 90 |
| b = 144.256 | ¦Â = 90 |
| c = 144.256 | ¦Ă = 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: 2010-03-02 Deposition Author(s): Nocek, B., Duggan, E., Abdullah, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
- This entry supersedes: 2QH8
Revision History (Full details and data files)
- Version 1.0: 2010-03-02
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary
