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1EIY

THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004826molecular_functionphenylalanine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006432biological_processphenylalanyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A0043039biological_processtRNA aminoacylation
A0046872molecular_functionmetal ion binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004826molecular_functionphenylalanine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006432biological_processphenylalanyl-tRNA aminoacylation
B0009328cellular_componentphenylalanine-tRNA ligase complex
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
BALA262
BASP452
BASP458
BGLU461
BGLU462

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b7y
ChainResidueDetails
AARG204
AALA314

site_idMCSA1
Number of Residues6
DetailsM-CSA 539
ChainResidueDetails
BALA149electrostatic stabiliser
BHIS178electrostatic stabiliser
BVAL204electrostatic stabiliser
BALA218electrostatic stabiliser
BHIS261steric role
BALA314steric role

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PDB entries from 2025-06-18

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