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3FHJ

Independent saturation of three TrpRS subsites generates a partially-assembled state similar to those observed in molecular simulations

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
A0016874molecular_functionligase activity
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
B0016874molecular_functionligase activity
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004830molecular_functiontryptophan-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006436biological_processtryptophanyl-tRNA aminoacylation
C0016874molecular_functionligase activity
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004830molecular_functiontryptophan-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006418biological_processtRNA aminoacylation for protein translation
D0006436biological_processtryptophanyl-tRNA aminoacylation
D0016874molecular_functionligase activity
E0000166molecular_functionnucleotide binding
E0004812molecular_functionaminoacyl-tRNA ligase activity
E0004830molecular_functiontryptophan-tRNA ligase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006412biological_processtranslation
E0006418biological_processtRNA aminoacylation for protein translation
E0006436biological_processtryptophanyl-tRNA aminoacylation
E0016874molecular_functionligase activity
F0000166molecular_functionnucleotide binding
F0004812molecular_functionaminoacyl-tRNA ligase activity
F0004830molecular_functiontryptophan-tRNA ligase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006412biological_processtranslation
F0006418biological_processtRNA aminoacylation for protein translation
F0006436biological_processtryptophanyl-tRNA aminoacylation
F0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRP A 1001
ChainResidue
APHE5
AGLY7
AGLN9
AVAL40
AHIS43
AMET129
AASP132
AILE133
AAMP1003

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRP D 1001
ChainResidue
DPHE5
DGLY7
DHIS43
DMET129
DASP132
DGLN147
DAMP1003

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP B 1001
ChainResidue
BPHE5
BGLY7
BVAL40
BHIS43
BMET129
BASP132
BILE133
BVAL141

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRP C 1001
ChainResidue
CPHE5
CGLY7
CGLN9
CVAL40
CHIS43
CMET129
CASP132
CILE133
CGLN147
CAMP1003

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP E 1001
ChainResidue
EGLN9
EVAL40
EHIS43
EMET129
EASP132
EILE133
EGLN147
EAMP1003

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRP F 1001
ChainResidue
FPHE5
FGLY7
FVAL40
FHIS43
FMET129
FASP132
FILE133
FVAL141
FGLN147
FAMP1003

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 1002
ChainResidue
ASER194
ALYS195
AAMP1003

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP A 1003
ChainResidue
AGLY17
AASN18
AGLY21
APRO142
AASP146
AILE176
AALA181
AILE183
ALYS192
AMET193
ATRP1001
APO41002

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 D 1002
ChainResidue
DASN18
DLYS192
DSER194
DLYS195
DAMP1003

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AMP D 1003
ChainResidue
DGLY17
DASN18
DILE176
DILE183
DLYS192
DMET193
DTRP1001
DPO41002

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1002
ChainResidue
BTHR15
BASN18
BSER194
BLYS195
BSER196
BAMP1003

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AMP B 1003
ChainResidue
BGLY17
BASN18
BGLY21
BILE183
BPO41002

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 1002
ChainResidue
CMET193
CSER194
CLYS195
CSER196
CAMP1003

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AMP C 1003
ChainResidue
CASP146
CILE183
CLYS192
CMET193
CTRP1001
CPO41002
CGLY17
CASN18
CGLY144

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 E 1002
ChainResidue
EASN18
ESER194
ELYS195
EAMP1003

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AMP E 1003
ChainResidue
EGLY17
EASN18
EGLY21
EALA22
EILE183
ELYS192
EMET193
ETRP1001
EPO41002

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 F 1002
ChainResidue
FASN18
FLYS192
FSER194
FLYS195
FAMP1003

site_idBC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AMP F 1003
ChainResidue
FGLY17
FASN18
FGLY144
FILE183
FLYS192
FMET193
FLYS195
FTRP1001
FPO41002

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY
ChainResidueDetails
APRO10-TYR19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues58
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26555258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DK4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS192
ALYS195

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
DLYS192
DLYS195

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS192
BLYS195

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
CLYS192
CLYS195

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ELYS192
ELYS195

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
FLYS192
FLYS195

site_idMCSA1
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
BLYS192electrostatic stabiliser
BLYS195electrostatic stabiliser

site_idMCSA3
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
CLYS192electrostatic stabiliser
CLYS195electrostatic stabiliser

site_idMCSA4
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
DLYS192electrostatic stabiliser
DLYS195electrostatic stabiliser

site_idMCSA5
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
ELYS192electrostatic stabiliser
ELYS195electrostatic stabiliser

site_idMCSA6
Number of Residues2
DetailsM-CSA 481
ChainResidueDetails
FLYS192electrostatic stabiliser
FLYS195electrostatic stabiliser

246704

PDB entries from 2025-12-24

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