9O5M | pdb_00009o5m

Prenylated-FMN maturase PhdC from Mycolicibacterium fortuitum bound to prenylated flavin mononucleotide in the P1 space group


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.62 Å
  • R-Value Free: 
    0.196 (Depositor), 0.196 (DCC) 
  • R-Value Work: 
    0.168 (Depositor), 0.168 (DCC) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

Structure 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


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pyridoxamine 5'-phosphate oxidase putative domain-containing protein
A, B, C, D
168Mycolicibacterium fortuitumMutation(s): 0 
Gene Names: XA26_16660
UniProt
Find proteins for A0A0N9XAG5 (Mycolicibacterium fortuitum)
Explore A0A0N9XAG5 
Go to UniProtKB:  A0A0N9XAG5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0N9XAG5
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
4LU (Subject of Investigation/LOI)
Query on 4LU

Download Ideal Coordinates CCD File 
E [auth A],
G [auth B],
I [auth C],
K [auth D]
1-deoxy-5-O-phosphono-1-(3,3,4,5-tetramethyl-9,11-dioxo-2,3,8,9,10,11-hexahydro-7H-quinolino[1,8-fg]pteridin-12-ium-7-y l)-D-ribitol
C22 H30 N4 O9 P
KOUJZPGFPGLHCZ-IYOUNJFTSA-O
NA
Query on NA

Download Ideal Coordinates CCD File 
F [auth A],
H [auth B],
J [auth C],
L [auth D]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.62 Å
  • R-Value Free:  0.196 (Depositor), 0.196 (DCC) 
  • R-Value Work:  0.168 (Depositor), 0.168 (DCC) 
Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.552α = 69.95
b = 60.19β = 85.032
c = 65.053γ = 65.414
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
Aimlessdata scaling
PHASERphasing
REFMACrefinement
Cootmodel building

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation (NSF, United States)United StatesCHE 2203729
National Science Foundation (NSF, United States)United StatesCHE 1904759

Revision History  (Full details and data files)

  • Version 1.0: 2026-02-18
    Type: Initial release