Download MendeleyStructure and functional properties of the cold-adapted catalase from Acinetobacter sp. Ver3 native to the Atacama plateau in northern Argentina
Sartorio, M.G., Cortez, N., Gonzalez, J.M.(2021) Acta Crystallogr D Biol Crystallogr D77: 369-379
6PT7
Structure of KatE1 catalase from Acinetobacter sp. Ver3
- PDB DOI: https://doi.org/10.2210/pdb6PT7/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Acinetobacter sp. Ver3
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2019-07-15 Released: 2020-07-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- R-Value Free: 0.209
- R-Value Work: 0.174
- R-Value Observed: 0.176
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Catalase | 500 | Acinetobacter sp. Ver3 | Mutation(s): 0 Gene Names: CL42_01515 |  | |
UniProt | |||||
Find proteins for A0A031LXI5 (Acinetobacter sp. Ver3) Explore A0A031LXI5 Go to UniProtKB: A0A031LXI5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A031LXI5 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAP (Subject of Investigation/LOI) Query on NAP | B [auth A] | NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H28 N7 O17 P3 XJLXINKUBYWONI-NNYOXOHSSA-N |  | ||
| HEM (Subject of Investigation/LOI) Query on HEM | C [auth A] | PROTOPORPHYRIN IX CONTAINING FE C34 H32 Fe N4 O4 KABFMIBPWCXCRK-RGGAHWMASA-L |  | ||
| CL Query on CL | D [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| UNX Query on UNX | E [auth A], F [auth A], G [auth A] | UNKNOWN ATOM OR ION X |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| OMT Query on OMT | A | L-PEPTIDE LINKING | C5 H11 N O4 S |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- R-Value Free: 0.209
- R-Value Work: 0.174
- R-Value Observed: 0.176
- Space Group: I 41 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 112.538 | α = 90 |
| b = 112.538 | β = 90 |
| c = 314.634 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2020-07-22 Deposition Author(s): Gonzalez, J.M., Sartorio, M.G., Cortez, N.
Revision History (Full details and data files)
- Version 1.0: 2020-07-22
Type: Initial release - Version 1.1: 2021-03-10
Changes: Database references - Version 1.2: 2023-10-11
Changes: Data collection, Database references, Refinement description
