Download MendeleyHomolytic versus heterolytic dioxygen bond cleavage in cytochrome P450 BM3.
Katayama, J.H., Roberts, A., Kaspera, R., Le Trong, I., Stenkamp, R.E., Thompson, J., Totah, R.A.To be published.
3DGI
Crystal structure of F87A/T268A mutant of CYP BM3
- PDB DOI: https://doi.org/10.2210/pdb3DGI/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Priestia megaterium
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2008-06-13 Released: 2009-06-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.220
- R-Value Work: 0.177
- R-Value Observed: 0.179
Starting Model: experimental
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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 |
| Bifunctional P-450/NADPH-P450 reductase | 461 | Priestia megaterium | Mutation(s): 2 Gene Names: CYP102A1, cyp102 EC: 1.14.14.1 (PDB Primary Data), 1.6.2.4 (UniProt) |  | |
UniProt | |||||
Find proteins for P14779 (Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)) Explore P14779 Go to UniProtKB: P14779 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P14779 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| HEM Query on HEM | C [auth A], E [auth B] | PROTOPORPHYRIN IX CONTAINING FE C34 H32 Fe N4 O4 KABFMIBPWCXCRK-RGGAHWMASA-L |  | ||
| DMS Query on DMS | D [auth A], F [auth B] | DIMETHYL SULFOXIDE C2 H6 O S IAZDPXIOMUYVGZ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.220
- R-Value Work: 0.177
- R-Value Observed: 0.179
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 58.934 | α = 90 |
| b = 146.625 | β = 97.36 |
| c = 63.515 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| CrystalClear | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2009-06-16 Deposition Author(s): Le Trong, I., Katayama, J.H., Totah, R.A., Stenkamp, R.E., Fox, E.P.
Revision History (Full details and data files)
- Version 1.0: 2009-06-16
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2021-10-20
Changes: Database references, Derived calculations - Version 1.3: 2023-08-30
Changes: Data collection, Refinement description
