Download MendeleySide-Chain Stacking and Beta-Helix Stability in P22 Tailspike Protein
Becker, M., Mueller, J.J., Weikl, T., Heinemann, U., Seckler, R.To be published.
2VFP | pdb_00002vfp
Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L
- PDB DOI: https://doi.org/10.2210/pdb2VFP/pdb
- Classification: HYDROLASE
- Organism(s): Lederbergvirus P22
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-11-05 Released: 2008-12-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.152 (Depositor), 0.160 (DCC)
- R-Value Work: 0.123 (Depositor), 0.140 (DCC)
- R-Value Observed: 0.125 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.3 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 |
| P22 TAILSPIKE PROTEIN | 559 | Lederbergvirus P22 | Mutation(s): 1 EC: 3.2.1 |  | |
UniProt | |||||
Find proteins for P12528 (Salmonella phage P22) Explore P12528 Go to UniProtKB: P12528 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P12528 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | H [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | B [auth A] C [auth A] D [auth A] E [auth A] F [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CA Query on CA | I [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.152 (Depositor), 0.160 (DCC)
- R-Value Work: 0.123 (Depositor), 0.140 (DCC)
- R-Value Observed: 0.125 (Depositor)
Space Group: P 21 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 120.29 | α = 90 |
| b = 120.29 | β = 90 |
| c = 120.29 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2008-12-16 Deposition Author(s): Becker, M., Mueller, J.J., Heinemann, U., Seckler, R.
Revision History (Full details and data files)
- Version 1.0: 2008-12-16
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2023-12-13
Changes: Data collection, Database references, Derived calculations, Other, Refinement description
