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4HJX

Crystal structure of F2YRS complexed with F2Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
A0016874molecular_functionligase activity
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004831molecular_functiontyrosine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006437biological_processtyrosyl-tRNA aminoacylation
B0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F2Y A 401
ChainResidue
AARG32
AHOH529
AGLY34
AGLU36
AALA67
AILE137
ATYR151
AGLN155
AASN158
AGLN173

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F2Y B 401
ChainResidue
BARG32
BGLY34
BGLU36
BALA67
BILE137
BTYR151
BGLN155
BASN158
BGLN173
BHOH523

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGkIHLGHY
ChainResidueDetails
APRO37-TYR46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12754495
ChainResidueDetails
AARG32
AGLU36
AGLN173
BARG32
BGLU36
BGLN173

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
ASER207
BSER207

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with t-RNA
ChainResidueDetails
AASN143
BASN143

218853

PDB entries from 2024-04-24

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