Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3N9I

Crystal structure of tryptophanyl-tRNA synthetase from Yersinia pestis CO92

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
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
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AGLY21
AVAL54
AMET144
AASP147

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BHOH516
AGLU299
BTYR247
BHOH354
BHOH487
BHOH515

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGeLTIGNY
ChainResidueDetails
APRO24-TYR33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140
ChainResidueDetails
BASP147
BGLY159
BVAL198
BLYS207
AGLN23
AGLY31
AASP147
AGLY159
AVAL198
ALYS207
BGLN23
BGLY31

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon