Structure of PDB 6f89 Chain B Binding Site BS01

Receptor Information

>6f89 Chain B (length=326) Species: 272844 (Pyrococcus abyssi GE5)

MTIIINVRERIEEWKIRIAAGFIREGKLVAFPTETVYGLGANALDENAVK
RIFEAKGRPADNPLIIHIASFEQLEVLAKEIPEEAEMLAKRFWPGPLTLV
LPKSEVVPRVITGGLDTVAVRMPAHEIALKLIELSERPIAAPSANISGKP
SPTSAHHVAEDFYGKIECIIDGGETRIGVESTVIDLTEWPPVLLRPGGLP
LEEIEKVIGEIRIHPAVYGKSVAEVIVVEGPRDKVRRKIEELIAKFKEEG
KKVGVIGSGSYDADEVFYLGDTVEEIARNLFKALRHMDRTGVDVILAEGV
EEKGLGLAVMNRLRKASGYRIIKVHH

Ligand information

• Ligand ID: BCT
• InChI: InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
• InChIKey: BVKZGUZCCUSVTD-UHFFFAOYSA-M
• SMILES:
  OpenEye OEToolkits 1.5.0: C(=O)(O)[O-]
  CACTVS 3.341: OC([O-])=O
  ACDLabs 10.04: [O-]C(=O)O
• Formula: C H O3
• Name: BICARBONATE ION
• PDB chain: 6f89 Chain B Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6f89 Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.
• Resolution: 2.81 Å
• Binding residue (original residue number in PDB): S143 R195
• Binding residue (residue number reindexed from 1): S143 R195
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 2.7.7.87: L-threonylcarbamoyladenylate synthase.

Gene Ontology

Molecular Function

• GO:0000049 tRNA binding
• GO:0003725 double-stranded RNA binding
• GO:0005524 ATP binding
• GO:0016779 nucleotidyltransferase activity
• GO:0061710 L-threonylcarbamoyladenylate synthase

Biological Process

• GO:0002949 tRNA threonylcarbamoyladenosine modification
• GO:0006450 regulation of translational fidelity
• GO:0008033 tRNA processing

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:6f89, PDBe:6f89, PDBj:6f89
• PDBsum: 6f89
• PubMed: 29650678
• UniProt: Q9UYB2|SUA5_PYRAB Threonylcarbamoyl-AMP synthase (Gene Name=sua5)