Download MendeleyAndrostenedione-bound structure of CYP154C2 from Streptomyces avermitilis in an open conformation
Xu, L.H., Fushinobu, S.To be published.
7CL9
Androstenedione-bound structure of CYP154C2 from Streptomyces avermitilis in an open conformation
- PDB DOI: https://doi.org/10.2210/pdb7CL9/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Streptomyces avermitilis MA-4680 = NBRC 14893
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2020-07-20 Released: 2021-07-21
- Funding Organization(s): National Natural Science Foundation of China (NSFC)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.249
- R-Value Work: 0.192
- R-Value Observed: 0.195
Starting Model: experimental
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This is version 2.1 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 |
| Cytochrome P450 hydroxylase | 400 | Streptomyces avermitilis MA-4680 = NBRC 14893 | Mutation(s): 0 Gene Names: cyp19, SAVERM_3882 |  | |
UniProt | |||||
Find proteins for Q82GL5 (Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)) Explore Q82GL5 Go to UniProtKB: Q82GL5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q82GL5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| HEM Query on HEM | B [auth A] | PROTOPORPHYRIN IX CONTAINING FE C34 H32 Fe N4 O4 KABFMIBPWCXCRK-RGGAHWMASA-L |  | ||
| ASD Query on ASD | C [auth A] | 4-ANDROSTENE-3-17-DIONE C19 H26 O2 AEMFNILZOJDQLW-QAGGRKNESA-N |  | ||
| PEG Query on PEG | D [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.249
- R-Value Work: 0.192
- R-Value Observed: 0.195
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 54.6 | α = 90 |
| b = 80.13 | β = 90 |
| c = 120.63 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| iMOSFLM | data reduction |
| SCALA | data scaling |
| MOLREP | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2021-07-21 Deposition Author(s): Xu, L.H., Fushinobu, S.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Natural Science Foundation of China (NSFC) | China | 81402810 |
Revision History (Full details and data files)
- Version 1.0: 2021-07-21
Type: Initial release - Version 2.0: 2023-09-20
Type: Coordinate replacement
Reason: Atoms with unrealistic or zero occupancies
Changes: Atomic model, Author supporting evidence, Data collection, Database references, Derived calculations, Non-polymer description, Refinement description, Source and taxonomy, Structure summary - Version 2.1: 2023-11-29
Changes: Refinement description
