Structure of PDB 4ttv Chain A

Receptor sequence
>4ttvA (length=403) Species: 9606 (Homo sapiens) [Search protein sequence]
SDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQ
EVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAME
QIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLE
NSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIR
FNLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQ
VMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNKKIRNAQLAQY
NFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
3D structure
PDB4ttv Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C413 R442 Q460 D462 H464 K543 H590
Catalytic site (residue number reindexed from 1) C93 R122 Q140 D142 H144 K223 H270
Enzyme Commision number 6.1.1.3: threonine--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 BC9 A G387 H388 R442 Y540 D564 L567 H590 G67 H68 R122 Y220 D244 L247 H270 PDBbind-CN: -logKd/Ki=6.68,IC50=209nM
BS02 ZN A H464 H590 H144 H270
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ttv, PDBe:4ttv, PDBj:4ttv
PDBsum4ttv
PubMed26271225
UniProtP26639|SYTC_HUMAN Threonine--tRNA ligase 1, cytoplasmic (Gene Name=TARS1)

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