Download MendeleyCrystal structure of the complex formed between phospholipase A2 and peptide Ala-Val-Tyr-Ser at 2.0 A resolution
Kumar, S., Singh, N., Sharma, S., Kaur, P., Singh, T.P.To be published.
2PB8 | pdb_00002pb8
Crystal structure of the complex formed between phospholipase A2 and peptide Ala-Val-Tyr-Ser at 2.0 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2PB8/pdb
- Classification: HYDROLASE
- Organism(s): Daboia russelii pulchella
- Mutation(s): No
- Deposited: 2007-03-28 Released: 2007-04-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.218 (Depositor)
- R-Value Work: 0.177 (Depositor)
- R-Value Observed: 0.179 (Depositor)
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| Phospholipase A2 VRV-PL-VIIIa | 121 | Daboia russelii pulchella | Mutation(s): 0 EC: 3.1.1.4 |  | |
UniProt | |||||
Find proteins for P59071 (Daboia russelii) Explore P59071 Go to UniProtKB: P59071 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P59071 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| AVYS | B [auth P] | 4 | N/A | Mutation(s): 0 |  |
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACT Query on ACT | C [auth A], D [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.218 (Depositor)
- R-Value Work: 0.177 (Depositor)
- R-Value Observed: 0.179 (Depositor)
Space Group: P 43
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 53.087 | α = 90 |
| b = 53.087 | β = 90 |
| c = 48.364 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MAR345 | data collection |
| DENZO | data reduction |
| SCALEPACK | data scaling |
| AMoRE | phasing |
Entry History
Deposition Data
- Released Date: 2007-04-17 Deposition Author(s): Kumar, S., Singh, N., Sharma, S., Kaur, P., Singh, T.P.
Revision History (Full details and data files)
- Version 1.0: 2007-04-17
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-10-18
Changes: Refinement description - Version 1.4: 2023-10-25
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.5: 2024-10-30
Changes: Structure summary
