Table 4 Interaction profile between PS and ATP in wild-type and alanine mutants after MD simulations.

From: Alanine mutation of the catalytic sites of Pantothenate Synthetase causes distinct conformational changes in the ATP binding region

Systems

No. of hydrogen bond

Participating residues in hydrogen bond with their bond length (Å)

Participating residues in hydrophobic bonding

Wild-type

16

Arg44(2.7 Å), Arg47(2.7 Å, 2.9 Å), Gly158(2.7 Å,), Lys160(2.5 Å, 2.9 Å), Val187(3.0 Å, 3.0 Å), Met195(2.9 Å), Ser196(2.7 Å), Ser197(3.1 Å, 2.8 Å, 2.6 Å), Arg198(2.8 Å, 2.7 Å, 2.5 Å)

Gly46, Leu50, Phe157, Pro185, Thr186

H44A

13

Arg47(2.6 Å), Lys160(2.5 Å, 3.0 Å), Asp161(2.5 Å), Val187(2.9 Å, 2.9 Å), Met195(2.9 Å), Ser196(2.7 Å), Ser197(2.9 Å, 3.0 Å), Arg198(3.2 Å, 2.6 Å, 2.5 Å)

Gly46, Phe157, Gly158, Pro185, Thr186

H47A

9

Arg44(2.8 Å), Gly158(2.9 Å,), Lys160(2.7 Å), Val187(2.9 Å, 3.1 Å), Met195(2.9 Å), Ser196(2.6 Å), Arg198(2.6 Å, 2.5 Å)

Gly46, His47, Leu50, Phe157, Pro185, Thr186

N69A

12

Arg44(2.6 Å), Lys160(2.9 Å, 2.6 Å, 2.9 Å), Val187(3.0 Å, 3.0 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.7 Å), Arg198(2.8 Å, 2.6 Å, 2.5 Å)

Met40, Gly46, His47, Leu50, Phe157, Gly158, Thr186

Q72A

16

Arg44(2.7 Å), Arg47(2.6 Å), Gly158(3.0 Å), Lys160(2.5 Å, 2.9 Å), Asp161(2.9 Å),Val187(2.9 Å, 2.8 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.9 Å, 2.9 Å, 3.1 Å), Arg198(2.7 Å, 2.7 Å, 3.1 Å)

His44, Leu50, Phe157, Pro185, Thr186

K160A

9

Arg44(2.6 Å), Val187(2.9 Å), Met195(2.8 Å, 3.3 Å), Ser197(3.2 Å, 2.8 Å), Arg198(2.9 Å, 2.9 Å, 2.9 Å)

Gly46, His47, Leu50, Phe157, Ala160, Pro185, Thr186

Q164A

15

Arg44(2.6 Å), Gly158(2.9 Å, 3.3 Å), Lys160(2.5 Å, 2.8 Å), Asp161(3.2 Å) Val187(2.9 Å, 2.7 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.8 Å, 3.1 Å), Arg198(2.5 Å, 2.6 Å, 3.0 Å)

Met40, His47, Leu50, Phe157, Pro185, Thr186

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