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1H4Q

Prolyl-tRNA synthetase from Thermus thermophilus complexed with tRNApro(CGG), ATP and prolinol

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004827molecular_functionproline-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006433biological_processprolyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0046872molecular_functionmetal ion binding
A0140101molecular_functioncatalytic activity, acting on a tRNA
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004827molecular_functionproline-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006433biological_processprolyl-tRNA aminoacylation
B0016874molecular_functionligase activity
B0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
B0046872molecular_functionmetal ion binding
B0140101molecular_functioncatalytic activity, acting on a tRNA
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1479
ChainResidue
ACYS427
ACYS432
ACYS458
ACYS461

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1481
ChainResidue
AARG312
AHIS323
ALEU324

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1479
ChainResidue
BCYS458
BCYS461
BCYS427
BCYS432

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1481
ChainResidue
BARG312
BHIS323
BLEU324

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ATP A1478
ChainResidue
AARG142
AGLU144
AARG152
APHE156
ATRP158
AGLN225
AALA226
AGLY227
ATHR228
AHIS230
ASER262
AARG264
APRI1480

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PRI A1480
ChainResidue
ATHR111
AGLU113
AARG142
ATRP158
APHE205
AHIS230
ASER258
ATRP259
AGLY260
AATP1478

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP B1478
ChainResidue
BARG142
BGLU144
BLEU151
BARG152
BTRP158
BGLN225
BALA226
BGLY227
BTHR228
BSER262
BARG264
BPRI1480

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PRI B1480
ChainResidue
BTHR111
BGLU113
BARG142
BTRP158
BPHE205
BHIS230
BSER258
BATP1478

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues58
DetailsRegion: {"description":"Interaction with tRNA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11399074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11399074","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10970866","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11399074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
AARG142

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
BARG142

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PDB entries from 2025-12-17

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