Download MendeleyKynurenine monooxygenase from Pseudomonas fluorescens complexed with 4-chlorophenylacetyltetrazole
Phillips, R.S., Ma, W.To be published.
9B2Y | pdb_00009b2y
Kynurenine monooxygenase from Pseudomonas fluorescens complexed with 4-chlorophenylacetyltetrazole
- PDB DOI: https://doi.org/10.2210/pdb9B2Y/pdb
- Classification: FLAVOPROTEIN/INHIBITOR
- Organism(s): Pseudomonas fluorescens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2024-03-17 Released: 2025-08-27
- Funding Organization(s): Not funded
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.246 (Depositor), 0.245 (DCC)
- R-Value Work: 0.205 (Depositor), 0.205 (DCC)
- R-Value Observed: 0.207 (Depositor)
Starting Model: experimental
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This is version 1.0 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 |
| Kynurenine 3-monooxygenase | 461 | Pseudomonas fluorescens | Mutation(s): 2 Gene Names: kmo, qbsG EC: 1.14.13.9 |  | |
UniProt | |||||
Find proteins for Q84HF5 (Pseudomonas fluorescens) Explore Q84HF5 Go to UniProtKB: Q84HF5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q84HF5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FAD (Subject of Investigation/LOI) Query on FAD | C [auth A], D [auth B] | FLAVIN-ADENINE DINUCLEOTIDE C27 H33 N9 O15 P2 VWWQXMAJTJZDQX-UYBVJOGSSA-N |  | ||
| A1AI5 (Subject of Investigation/LOI) Query on A1AI5 | F [auth B] | 1-(3-chlorophenyl)-2-(2H-tetrazol-5-yl)ethan-1-one C9 H7 Cl N4 O ABPAVOQJRPASKZ-UHFFFAOYSA-N |  | ||
| CL Query on CL | E [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.246 (Depositor), 0.245 (DCC)
- R-Value Work: 0.205 (Depositor), 0.205 (DCC)
- R-Value Observed: 0.207 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 69.41 | α = 90 |
| b = 51.66 | β = 103.86 |
| c = 134.98 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| autoPROC | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-08-27 Deposition Author(s): Phillips, R.S., Ma, W.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Not funded | -- |
Revision History (Full details and data files)
- Version 1.0: 2025-08-27
Type: Initial release
