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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