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. 2008 Feb 14;36(5):e29. doi: 10.1093/nar/gkn008

Table 3.

Predicted RNA-binding residues in aminoacyl–tRNA–synthetases

PDB-chain Binding site Predicted RNA-binding residues
1h3f-A Patch I168−Y175, A178, Q179
Clefta L42, G43–D45, P46−D50, H52, G54, H55, V58, G77, F79, Y108, Q111, R155−D157, H171, E172, Y175, A178, Q179, G194, D196, Q197, N200, P222, L223, V225, R230, E231, K232, S234, K235, S236, I237, Y240, T244 −P246
1hc7-A Patchb S15, L19, Y30–T36, S88, E90, L91, E113, T114, R142, W143, E144, M145–R148, L151, R152, E155, F156, L157, W158, K199, K202–F205, A206, G207, Q225, A226, T228, H230, L232, N235, F236, S258, G260, S262, W263, R264, Q437, E438, T441, T443, A476, Y477
Cleft I37–V39, Y44, L70, F71, F87, P89, A92, V93, V108, N139, V141, W143, E155, L157
1j09-A Patch L235, R237, N238, P239, D240, K241, T242, K243, I244, S245, K246, R247, K248, S249, H250
Cleftc A7, S9, P10, T11, G12, D13, H15, G17, T18, I21, E41, D42, T43, D44, R45, A46, R47, V49, K180, Y184, T186, Y187, A206, E208, W209, L235, K243, I244, S245, K246, R247, S249, H250, S252, W255

aResidues in bold underlined are involved in binding ATP or tyrosinol based on the corresponding structure of tyrosyl-tRNA synthetase complexed with its cognate tRNATyr, ATP and tyrosinol (1h3e-A).

bResidues in bold underlined are involved in binding ATP or prolinol based on the corresponding structure of prolyl-tRNA synthetase complexed with its cognate tRNAPro, ATP and prolinol (1h4q-A).

cResidues in bold underlined are involved in binding the tRNA 3′-terminal CytCytAde based on the structure of glutamyl-tRNA synthetase complexed with its cognate tRNAGlu and glutamol-AMP (1n78-A).