Download MendeleyThe crystal structure of Se-AsfvPolX(L52/163M mutant) in complex with 1nt-gap DNA1
Chen, Y.Q., Zhang, J., Gan, J.H.To be published.
5HR9 | pdb_00005hr9
The crystal structure of Se-AsfvPolX(L52/163M mutant) in complex with 1nt-gap DNA1
- PDB DOI: https://doi.org/10.2210/pdb5HR9/pdb
- NAKB: 5HR9
- Classification: TRANSFERASE/DNA
- Organism(s): African swine fever virus, synthetic construct
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2016-01-23 Released: 2017-01-18
- Funding Organization(s): National Natural Science Fundation of China
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.256 (Depositor), 0.260 (DCC)
- R-Value Work: 0.206 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.209 (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 |
| DNA polymerase beta-like protein | 178 | African swine fever virus | Mutation(s): 2 Gene Names: O174L EC: 2.7.7.7 |  | |
UniProt | |||||
Find proteins for P42494 (African swine fever virus (strain Badajoz 1971 Vero-adapted)) Explore P42494 Go to UniProtKB: P42494 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P42494 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar nucleic acids by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | Organism | Image | |
| DNA (5'-D(*GP*GP*AP*CP*AP*AP*CP*GP*GP*GP*AP*CP*AP*AP*C)-3') | 15 | synthetic construct |  | ||
Sequence AnnotationsExpand | |||||
| |||||
Find similar nucleic acids by: Sequence | 3D Structure
Small Molecules
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.256 (Depositor), 0.260 (DCC)
- R-Value Work: 0.206 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.209 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 74.323 | ¦Á = 90 |
| b = 82.24 | ¦Â = 90 |
| c = 101.416 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHENIX | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2017-01-18 Deposition Author(s): Chen, Y.Q., Zhang, J., Gan, J.H.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Natural Science Fundation of China | China | 31370728 |
Revision History (Full details and data files)
- Version 1.0: 2017-01-18
Type: Initial release - Version 1.1: 2024-11-06
Changes: Data collection, Database references, Structure summary
