Structure of PDB 1ozq Chain A

Receptor sequence

>1ozqA (length=372) Species: 542 (Zymomonas mobilis)

RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVR
ATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGFQVMS
LSSLTKQSEEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTP
YPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENL
RQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLM
GVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSED
LKPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQK
IRDSISEGRFSQFAQDFRARYF

3D structure

• PDB: 1ozq Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D102 D280 C318 C320 C323 H349
• Catalytic site (residue number reindexed from 1): D92 D270 C308 C310 C313 H339
• Enzyme Commision number: 2.4.2.29: tRNA-guanosine(34) preQ1 transglycosylase.

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	ZN	A	C318 C320 C323 H349	C308 C310 C313 H339
BS02	PRF	A	F106 D156 G229 L231 M260	F96 D146 G219 L221 M250

Gene Ontology

Molecular Function

• GO:0008479 tRNA-guanosine(34) queuine transglycosylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0002099 tRNA wobble guanine modification
• GO:0006400 tRNA modification
• GO:0008033 tRNA processing
• GO:0008616 queuosine biosynthetic process
• GO:0101030 tRNA-guanine transglycosylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1ozq, PDBe:1ozq, PDBj:1ozq
• PDBsum: 1ozq
• PubMed: 14523925
• UniProt: P28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)