Download MendeleyTarget-binding to S100A5 changes Ca(2+)-binding affinity and dynamics.
Liriano, M.A., Varney, K.M., Ishima, R., Toth, E.A., Weber, D.J.To be published.
4DIR | pdb_00004dir
2.6 Angstrom X-ray structure of human CA(2+)-S100A5
- PDB DOI: https://doi.org/10.2210/pdb4DIR/pdb
- Classification: METAL BINDING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-01-31 Released: 2013-02-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.283 (Depositor), 0.290 (DCC)
- R-Value Work: 0.243 (Depositor), 0.230 (DCC)
- R-Value Observed: 0.245 (Depositor)
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 |
| Protein S100-A5 | 92 | Homo sapiens | Mutation(s): 0 Gene Names: S100A5, S100D |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P33763 (Homo sapiens) Explore P33763 Go to UniProtKB: P33763 | |||||
PHAROS: P33763 GTEx: ENSG00000196420 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P33763 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CA Query on CA | C [auth A], D [auth A], E [auth B], F [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.283 (Depositor), 0.290 (DCC)
- R-Value Work: 0.243 (Depositor), 0.230 (DCC)
- R-Value Observed: 0.245 (Depositor)
Space Group: P 41
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 52.692 | α = 90 |
| b = 52.692 | β = 90 |
| c = 67.012 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASES | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2013-02-13 Deposition Author(s): Liriano, M.A., Toth, E.A., Weber, D.J.
Revision History (Full details and data files)
- Version 1.0: 2013-02-13
Type: Initial release - Version 1.1: 2024-02-28
Changes: Data collection, Database references, Derived calculations
