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3TZE

Crystal structure of a tryptophanyl-tRNA synthetase from Encephalitozoon cuniculi bound to tryptophan

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004830molecular_functiontryptophan-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRP A 386
ChainResidue
ATYR84
ATHR85
AGLY86
AGLN119
ATHR121
AGLU124
AGLU206
AVAL226
AGLN232

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 387
ChainResidue
ASER212
APHE215
AILE218

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRP B 386
ChainResidue
BTYR84
BGLY86
BARG87
BGLY88
BGLN119
BGLU124
BLYS125
BGLU206
BALA228
BGLN232
BPHE236

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 387
ChainResidue
BSER212
BPHE215
BILE218

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SKtMHIGHT
ChainResidueDetails
APRO89-THR99

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PDB entries from 2024-07-24

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