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2PID

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004831molecular_functiontyrosine-tRNA ligase activity
B0005524molecular_functionATP binding
B0006418biological_processtRNA aminoacylation for protein translation
B0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE YSA A 384
ChainResidue
ATYR77
AGLN225
AASP228
AGLN241
AGLY243
AGLY244
AASP246
AGLN247
APRO272
ALEU273
AILE274
AGLY79
AHOH388
AHOH400
AHOH403
AASP81
AGLY90
AHIS91
ALEU111
ATHR116
AASP121
ATYR221

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE YSA B 384
ChainResidue
BTYR77
BGLY79
BASP81
BGLY90
BHIS91
BALA94
BLEU111
BTHR116
BASP121
BTYR221
BGLN225
BASP228
BGLN241
BGLY243
BGLY244
BASP246
BGLN247
BPRO272
BLEU273
BILE274
BHOH397

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHVGHL
ChainResidueDetails
APRO82-LEU92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17997975, ECO:0007744|PDB:2PID, ECO:0007744|PDB:3ZXI
ChainResidueDetails
ATYR77
AASP81
AASP121
AILE274
BTYR77
BASP81
BASP121
BILE274

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:17997975, ECO:0007744|PDB:2PID
ChainResidueDetails
ATYR221
BGLN247
AGLN225
AASP228
AGLY244
AGLN247
BTYR221
BGLN225
BASP228
BGLY244

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS284
BLYS284

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS355
BLYS355

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BYL4
ChainResidueDetails
ALYS367
BLYS367

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ts1
ChainResidueDetails
AARG129
AARG125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ts1
ChainResidueDetails
BARG129
BARG125

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PDB entries from 2025-06-18

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