Download MendeleyStructure and Mechanism of the Prenylated-FMN Maturase, PhdC
DiRocco, D.J., Kilde, I., Langford, D.P., Roy, P., Bhaumik, S., Mendoza, J., Koutmos, M., Marsh, E.N.G.(2026) ACS Catal 16: 1773-1782
9NK3 | pdb_00009nk3
Prenylated-FMN maturase PhdC E45A mutant from Mycolicibacterium fortuitum (apo)
- PDB DOI: https://doi.org/10.2210/pdb9NK3/pdb
- Classification: FLAVOPROTEIN
- Organism(s): Mycolicibacterium fortuitum
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2025-02-28 Released: 2026-02-18
- Funding Organization(s): National Science Foundation (NSF, United States)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.32 Å
- R-Value Free: 0.146 (Depositor), 0.146 (DCC)
- R-Value Work: 0.120 (Depositor), 0.120 (DCC)
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Pyridoxamine 5'-phosphate oxidase putative domain-containing protein | 168 | Mycolicibacterium fortuitum | Mutation(s): 1 Gene Names: XA26_16660 |  | |
UniProt | |||||
Find proteins for A0A0N9XAG5 (Mycolicibacterium fortuitum) Explore A0A0N9XAG5 Go to UniProtKB: A0A0N9XAG5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0N9XAG5 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MRD Query on MRD | D [auth A] | (4R)-2-METHYLPENTANE-2,4-DIOL C6 H14 O2 SVTBMSDMJJWYQN-RXMQYKEDSA-N |  | ||
| EDO Query on EDO | C [auth A], E [auth A], F [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| NA Query on NA | B [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.32 Å
- R-Value Free: 0.146 (Depositor), 0.146 (DCC)
- R-Value Work: 0.120 (Depositor), 0.120 (DCC)
Space Group: I 2 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 59.801 | α = 90 |
| b = 75.605 | β = 90 |
| c = 80.895 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| Aimless | data scaling |
| autoPROC | data reduction |
| PHASER | phasing |
| Coot | model building |
Entry History & Funding Information
Deposition Data
- Released Date: 2026-02-18 Deposition Author(s): Kilde, I.R., Koutmos, M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Science Foundation (NSF, United States) | United States | CHE 2203729 |
| National Science Foundation (NSF, United States) | United States | CHE 1904759 |
Revision History (Full details and data files)
- Version 1.0: 2026-02-18
Type: Initial release
