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Table 3 Predicted function/contacts of conserved residues. Homologous residues making similar contacts in different structures are in the same rows. Interacting functional groups are indicated in parentheses ("b" denotes backbone). Contacts absent from the lowest-energy solution, but present in other "top 20" solutions are shown in italics.

From: Characterization of the cofactor-binding site in the SPOUT-fold methyltransferases by computational docking of S-adenosylmethionine to three crystal structures

 

Structure:

1gz0

1ipa

1k3r

a) AdoMet-binding

adenine

A175

T194

S190

  

G201

G220

G223

 

ribose O2

M202 (bNH)

L221(bNH)

L224(bNH)

 

ribose O3

G196(bNH)

G215(bNH)

G218(bNH)

  

T174(OH)

T193(bCO)

T189(bCO)

 

methionine COO -

I216(bNH)

I235(bNH)

L236(bNH)

    

T235(bNH)

 

methionine NH 3 +

I216(bCO)

I235(bCO)

 
    

N234(OD1)

    

Q239(OE1)

b) target binding & catalysis

(precise role unknown)

N108

N129

K27

  

E198

E217

P220

  

S224

S243

T243

  

N226

N245

R245

    

T246

  

S228

S247

E247

  

R114 (2nd subunit)

R135 (2nd subunit)

R33 (2nd subunit)