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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
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
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004830molecular_functiontryptophan-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006436biological_processtryptophanyl-tRNA aminoacylation
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004830molecular_functiontryptophan-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006412biological_processtranslation
D0006418biological_processtRNA aminoacylation for protein translation
D0006436biological_processtryptophanyl-tRNA aminoacylation
E0000166molecular_functionnucleotide binding
E0004812molecular_functionaminoacyl-tRNA ligase activity
E0004830molecular_functiontryptophan-tRNA ligase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0006412biological_processtranslation
E0006418biological_processtRNA aminoacylation for protein translation
E0006436biological_processtryptophanyl-tRNA aminoacylation
F0000166molecular_functionnucleotide binding
F0004812molecular_functionaminoacyl-tRNA ligase activity
F0004830molecular_functiontryptophan-tRNA ligase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0006412biological_processtranslation
F0006418biological_processtRNA aminoacylation for protein translation
F0006436biological_processtryptophanyl-tRNA aminoacylation
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 Residues36
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4
ChainResidueDetails
AGLN9
DGLY144
DILE183
DLYS192
BGLN9
BGLY17
BASP132
BGLY144
BILE183
BLYS192
CGLN9
AGLY17
CGLY17
CASP132
CGLY144
CILE183
CLYS192
EGLN9
EGLY17
EASP132
EGLY144
EILE183
AASP132
ELYS192
FGLN9
FGLY17
FASP132
FGLY144
FILE183
FLYS192
AGLY144
AILE183
ALYS192
DGLN9
DGLY17
DASP132

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 Residues3
DetailsM-CSA 481
ChainResidueDetails
ALYS111electrostatic stabiliser
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
DLYS111electrostatic stabiliser
DLYS192electrostatic stabiliser
DLYS195electrostatic stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
BLYS111electrostatic stabiliser
BLYS192electrostatic stabiliser
BLYS195electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
CLYS111electrostatic stabiliser
CLYS192electrostatic stabiliser
CLYS195electrostatic stabiliser

site_idMCSA5
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ELYS111electrostatic stabiliser
ELYS192electrostatic stabiliser
ELYS195electrostatic stabiliser

site_idMCSA6
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
FLYS111electrostatic stabiliser
FLYS192electrostatic stabiliser
FLYS195electrostatic stabiliser

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PDB entries from 2024-07-10

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