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Table 1 Structures used to model CaFADS and the interaction with its ligands.

From: Structural analysis of FAD synthetase from Corynebacterium ammoniagenes

  PDB SUBSTRATES (%) IDENTITIES (%) CONSERVATIVE SUBSTITUTIONS REFERENCE
FAD synthetases      
T. maritima 1mrz   29.3 40.2 [14]
N-terminala    30.6 39.2  
C-terminalb    27.6 41.5  
T. maritima complexed      
  1s4m RF 29.3 40.2 [15]
  1t6x ADP    
  1t6y FMN, ADP, AMP    
Nucleotydyltransferases a      
GCT B. subtilis 1coz CTP 12.4 23.1 [30]
NMNAT M. jannaschii 1f9a Mg2+, ATP 12.9 22.0 [32]
NMNAT H. sapiens 1kku   10.8 18.3 [31]
NMNAT M. thermoautotropicum 1ej2 NAD+, Na+ 13.0 22.6 [33]
PPAT E. coli 1b6t dPCoA 13.0 26.3 [34]
  1gn8 ATP, Mn2+    [37]
PPAT T. thermophilus 1od6 Ppant 11.3 22.0 [35]
Riboflavinkinases b      
H. sapiens 1p4m ADP, Mg2+, FMN 25.7 41.4 [21]
  1q9s ADP, Mg2+, FMN    [22]
  1nb0 ADP, Mg2+    [21]
S. pombe 1n06 ADP    [23]
  1n07 FMN, ADP 23 38.2  
  1n08 Zn2+, ADP    
  1. Parameters derived from the structure-based sequence alignment of the produced CaFADS models over structural databases.
  2. a Alignments with the segment 19–186 from CaFADS
  3. b Alignments with the segment 187–338 from CaFADS