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

1MB2

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation

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
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
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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP A 400
ChainResidue
APHE5
AGLY7
AVAL40
AHIS43
AMET129
AASP132
AVAL143
AGLN147

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP B 401
ChainResidue
BGLY7
BGLN9
BVAL40
BHIS43
BMET129
BASP132
BGLN147
BPHE5

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP C 402
ChainResidue
CPHE5
CGLY7
CVAL40
CHIS43
CMET129
CASP132
CVAL143
CGLN147

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRP D 403
ChainResidue
DPHE5
DGLY7
DGLN9
DVAL40
DHIS43
DMET129
DASP132
DVAL141
DGLN147

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRP E 404
ChainResidue
EPHE5
EGLY7
EHIS43
EMET129
EASP132
EVAL143
EGLN147

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP F 405
ChainResidue
FPHE5
FGLY7
FGLN9
FHIS43
FMET129
FASP132
FVAL143
FGLN147

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
BGLY144
BILE183
BLYS192
CGLN9
CGLY17
CASP132
CGLY144
CILE183
CLYS192
DGLN9
AGLY17
DGLY17
DASP132
DGLY144
DILE183
DLYS192
EGLN9
EGLY17
EASP132
EGLY144
EILE183
AASP132
ELYS192
FGLN9
FGLY17
FASP132
FGLY144
FILE183
FLYS192
AGLY144
AILE183
ALYS192
BGLN9
BGLY17
BASP132

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ALYS111electrostatic stabiliser
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
BLYS111electrostatic stabiliser
BLYS192electrostatic stabiliser
BLYS195electrostatic stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
CLYS111electrostatic stabiliser
CLYS192electrostatic stabiliser
CLYS195electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
DLYS111electrostatic stabiliser
DLYS192electrostatic stabiliser
DLYS195electrostatic 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

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon