Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 1h4t Chain C

Receptor sequence >1h4tC (length=464) Species: 274 (Thermus thermophilus) [Search protein sequence] KGLTPQSQDFSEWYLEVIQKAELADYGPVRGTIVVRPYGYAIWENIQQVL DRMFKETGHQNAYFPLFIPMSFLFSPELAVVTHAGGEELEEPLAVRPTSE TVIGYMWSKWIRSWRDLPQLLNQWGNVVRWEMRTRPFLRTSEFLWQEGHT AHATREEAEEEVRRMLSIYARLAREYAAIPVIEGLKTEKEKFAGAVYTTT IEALMKDGKALQAGTSHYLGENFARAFDIKFQDRDLQVKYVHTTSWGLSW RFIGAIIMTHGDDRGLVLPPRLAPIQVVIVPIYKDESRERVLEAAQGLRQ ALLAQGLRVHLDDRDQHTPGYKFHEWELKGVPFRVELGPKDLEGGQAVLA SRLGGKETLPLAALPEALPGKLDAFHEELYRRALAFREDHTRKVDTYEAF KEAVQEGFALAFHCGDKACERLIQEETTATTRCVPFEAEPEEGFCVRCGR PSAYGKRVVFAKAY

3D structure PDB 1h4t A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase Chain C Resolution 2.9 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) E113 R142 H162 Catalytic site (residue number reindexed from 1) E100 R129 H149 Enzyme Commision number 6.1.1.15: proline--tRNA ligase.

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 PRO C T111 E113 W158 E160 F205 H230 S258 W259 G260 T98 E100 W145 E147 F192 H217 S245 W246 G247 BS02 ZN C C427 C432 C458 C461 C414 C419 C445 C448

Gene Ontology Molecular Function GO:0000166 nucleotide binding GO:0004812 aminoacyl-tRNA ligase activity GO:0004827 proline-tRNA ligase activity GO:0005524 ATP binding GO:0046872 metal ion binding

	Biological Process
GO:0006412	translation
GO:0006418	tRNA aminoacylation for protein translation
GO:0006433	prolyl-tRNA aminoacylation

	Cellular Component
GO:0005737	cytoplasm
GO:0017101	aminoacyl-tRNA synthetase multienzyme complex

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component