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. 2021 Aug 24;11:17094. doi: 10.1038/s41598-021-96524-z

Table 3.

Amino acid residues involved in the establishment of PamTps1 active site pocket and catalysis activity predicted using CASTp and InterProScan.

Structure/Motif Residues Functions
N-terminal domain (RRx8W) R1R2S3G4N5Y6Q7P8SAW Active site lid
A–C loop (RxR) R259DR Active site lid
R259—Hydrogen bond donor
Helix C W268, Y272 Active site pocket
W268—Aromatic residue surrounding non-polar hydrocarbon of substrate
W268, Y272—Hydrophobic interaction with PPi
Helix D1 I288V289, L291V292T293 Active site pocket
V289, V292T293—Hydrophobic interaction with PPi
Helix D1(DDxxD) D296D297VY299D300 Active site pocket
D296, D300—metal binding motif
Helix F F371, E374A375, Y378Y379 Active site pocket
Helix G1 T396 Active site pocket
Turn I397A398 Active site pocket, hydrophobic interaction with PPi
Helix G2 A399, A401A402 Active site pocket
A399, A402—Hydrophobic interaction with PPi
Helix H (L,V)(V,L,A)(N,D)D(L,I,V)x(S,T)xxxE/DTE L436R437L438AD440D441LG F447E448, E450- Active site lid
Active site pocket
R437—Hydrogen bond donor
T444APF447E448, E450 D440, T444, E448 – metal binding motif
L436—Hydrophobic interaction with PPi
H-α1 loop R451G452D453V454A455 Active site lid
K456A457, V458 K456—Hydrogen bond donor
310 helix Y517 Active site pocket, hydrophobic interaction with PPi
J-K loop G520D521G522Y523G524V525 Active site lid
Y523—Aromatic residue surrounding non-polar hydrocarbon of substrate/Hydrophobic interaction with PPi