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3ZXI

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with a tyrosyl-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 Residues19
DetailsBINDING SITE FOR RESIDUE TYA A 1374
ChainResidue
ATYR77
ATYR221
AGLN225
AASP228
AGLY243
AGLY244
AASP246
AGLN247
APRO272
ALEU273
AILE274
AGLY79
AASP81
AHIS88
AGLY90
AHIS91
ALEU111
ATHR116
AASP121

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE TYA B 1374
ChainResidue
BTYR77
BGLY79
BASP81
BHIS88
BGLY90
BHIS91
BALA94
BLEU111
BTHR116
BASP121
BTYR221
BGLN225
BASP228
BGLN241
BGLY243
BGLY244
BASP246
BGLN247
BPRO272
BLEU273
BILE274

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 Residues18
DetailsMotif: {"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17997975","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PID","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17997975","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PID","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BYL4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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