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9QRP

Thermus thermophilus seryl-tRNA synthetase bound to tRNA(ser)(GGA) and seryl-adenylate analogue.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004828molecular_functionserine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006434biological_processseryl-tRNA aminoacylation
A0016260biological_processL-selenocysteine biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0070905molecular_functionserine binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004828molecular_functionserine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006434biological_processseryl-tRNA aminoacylation
B0016260biological_processL-selenocysteine biosynthetic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0070905molecular_functionserine binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 884
ChainResidueDetails
AARG256electrostatic stabiliser
AARG271electrostatic stabiliser
AGLU345metal ligand
ASER348metal ligand
AARG386electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 884
ChainResidueDetails
BARG256electrostatic stabiliser
BARG271electrostatic stabiliser
BGLU345metal ligand
BSER348metal ligand
BARG386electrostatic stabiliser

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PDB entries from 2026-03-25

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