Structure of PDB 5ztb Chain A

Receptor sequence
>5ztbA (length=307) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
VCKVCGQKAQVEMRSRGLALCREHYLDWFVKETERAIRRHRMLLPGERVL
VAVSGGKDSLALWDVLSRLGYQAVGLHIELGIGEYSKRSLEVTQAFARER
GLELLVVDLKEAYGFGVPELARLSGRVACSACGLSKRYIINQVAVEEGFR
VVATGHNLDDEAAVLFGNLLNPLSRQGPVLPEKPGLAARVKPFYRFSERE
VLSYTLLRGIRYLHEECPNAKGAKSLLYKEALNLVERSMPGAKLRFLDGF
LEKIRPRLALRECERCGYPTTGAVCAFCRMWDAVYRRAKKRKLLPEEVSF
RPRVKPL
3D structure
PDB5ztb The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus.
ChainA
Resolution2.2 Å
3D
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
Enzyme Commision number 2.8.1.15: tRNA-5-methyluridine(54) 2-sulfurtransferase.
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 SF4 A I83 C130 C133 C222 N224 I82 C129 C132 C217 N219
BS02 ZN A C6 C22 H25 C5 C21 H24
BS03 ZN A C274 C277 C286 C289 C263 C266 C275 C278
BS04 ATP A A53 V54 S55 G57 D59 S60 I79 K137 G156 H157 A52 V53 S54 G56 D58 S59 I78 K136 G155 H156
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0002098 tRNA wobble uridine modification
GO:0002143 tRNA wobble position uridine thiolation
GO:0008033 tRNA processing
GO:0034227 tRNA thio-modification
Cellular Component
GO:0002144 cytosolic tRNA wobble base thiouridylase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5ztb, PDBe:5ztb, PDBj:5ztb
PDBsum5ztb
PubMed32265486
UniProtQ72LF3|TTUA_THET2 tRNA-5-methyluridine(54) 2-sulfurtransferase (Gene Name=ttuA)

[Back to BioLiP]