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4J15

Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0004046molecular_functionaminoacylase activity
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004815molecular_functionaspartate-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006422biological_processaspartyl-tRNA aminoacylation
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0045202cellular_componentsynapse
A0065003biological_processprotein-containing complex assembly
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0004046molecular_functionaminoacylase activity
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004815molecular_functionaspartate-tRNA ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006422biological_processaspartyl-tRNA aminoacylation
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
B0045202cellular_componentsynapse
B0065003biological_processprotein-containing complex assembly
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AARG63
AALA64
AGLN82
AHOH783
AHOH876
BASP261
BGOL602
BHOH819

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
AVAL144
AILE145
ASER146
ALEU147
BASP434
BHOH852
ASER32

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AGLN199
AGLU474
ASER490
AMET491
APHE492
BGLN219
BPRO221

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
ALYS40
AGOL605
BHIS300
BARG345

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 605
ChainResidue
AGLN38
AGOL604
AHOH843
BARG408

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 601
ChainResidue
AHIS204
AARG207
AGLU208
AILE211
AHOH768
BHIS204
BARG207
BHOH799

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 602
ChainResidue
AARG63
AGLN82
AGOL601
BPHE295
BASN296
BHOH841

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 603
ChainResidue
ATYR297
BARG43
BASP115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU229
BARG281
BGLU424
BSER427
BARG431
BGLY472
AARG273
AARG281
AGLU424
ASER427
AARG431
AGLY472
BGLU229
BARG273

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR52
BTHR52

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS74
ALYS374
BLYS74
BLYS374

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER249
BSER249

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000255
ChainResidueDetails
ATHR500
BTHR500

237735

PDB entries from 2025-06-18

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