Structure of PDB 4p3n Chain B

Receptor sequence
>4p3nB (length=402) Species: 9606 (Homo sapiens) [Search protein sequence]
DHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQE
VVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFD
HRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQ
IEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLEN
SLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRF
NLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQV
MVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNKKIRNAQLAQYN
FILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAEE
EF
3D structure
PDB4p3n Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase.
ChainB
Resolution2.6 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) C92 R121 Q139 D141 H143 K222 H269
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 2CR B G387 H388 M411 R442 Y540 D564 L567 H590 G66 H67 M90 R121 Y219 D243 L246 H269
BS02 ZN B H464 H590 H143 H269
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:4p3n, PDBe:4p3n, PDBj:4p3n
PDBsum4p3n
PubMed25824639
UniProtP26639|SYTC_HUMAN Threonine--tRNA ligase 1, cytoplasmic (Gene Name=TARS1)

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