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2ZR3

Crystal structure of seryl-tRNA synthetase from Pyrococcus horikoshii

Replaces:  2DQ2
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004828molecular_functionserine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006434biological_processseryl-tRNA aminoacylation
A0016260biological_processselenocysteine biosynthetic process
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004828molecular_functionserine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006434biological_processseryl-tRNA aminoacylation
B0016260biological_processselenocysteine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00176
ChainResidueDetails
ATHR252
BGLU306
BGLU370
BTHR406
AARG283
AVAL299
AGLU306
AGLU370
ATHR406
BTHR252
BARG283
BVAL299

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
AASP292
AARG298
AGLU285
AARG283
ATHR288

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
BASP292
BARG298
BGLU285
BARG283
BTHR288

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
AARG283

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
BARG283

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PDB entries from 2024-07-24

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