Structure of PDB 2d6f Chain C

Receptor sequence

>2d6fC (length=485) Species: 145262 (Methanothermobacter thermautotrophicus)

MDWEKVGLKMGLEIHQQLDTESKLFCPCRTELTDSEPDHDIVRNLRPTAF
EEAMRKLHFHYENYHEETCLVEADEEPPHPLNPEALEIAVTIALLLNMRV
VDEFHTMRKQVIDGSNTGGFQRTGLVATDGHLETPQGTVKIENLCLEEDA
ARRIRETGDGVVFRLDRLGIPLVEITTDPSMSDPQQLREVAYQIGQILRS
TRVKRGLGTIRQDLNISIRDGARVEVKGVQDLDLIPEIVEREVKRQLSLV
EIRDTLQERGAVVEDKIFDVSEVFADTESRIISSAESVLAVKLRGFDGLI
GVEIQPGRRLGTEMADYAKKRGVSGIFHTDELPAYGITEEEVRGLRDAVG
ASQGDAVVMVAHERVTAENALREVIRRAEMAIQGVPEETRKALPDGNTQY
LRPLPTSSRMYLETDIPLFRIEDDLLEGIRRNLPELPSEKKERIMRDYGL
SEDLASQLVKRNLVDEFDTTVIASLLAYTLRELRR

3D structure

• PDB: 2d6f Structural basis of RNA-dependent recruitment of glutamine to the genetic code
• Chain: C
• Resolution: 3.15 Å

Enzymatic activity

• Enzyme Commision number: 6.3.5.-

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	rna	C	Q240 D241 S461 D463 Q467 Y496 R499 E500 R502	Q230 D231 S451 D453 Q457 Y478 R481 E482 R484
BS02	ZN	C	C28 C79 E82	C28 C69 E72

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004812 aminoacyl-tRNA ligase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
• GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity

Biological Process

• GO:0006412 translation
• GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2d6f, PDBe:2d6f, PDBj:2d6f
• PDBsum: 2d6f
• PubMed: 16809540
• UniProt: O26803|GATE_METTH Glutamyl-tRNA(Gln) amidotransferase subunit E (Gene Name=gatE)