Structure of PDB 1t43 Chain A

Receptor sequence
>1t43A (length=274) Species: 562 (Escherichia coli) [Search protein sequence]
EYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQ
CQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQ
ALARLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQR
NAQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRF
EPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFI
LAGYHDVETCRDYGDNERVTLGRY
3D structure
PDB1t43 Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L89 N183 P184
Catalytic site (residue number reindexed from 1) L88 N182 P183
Enzyme Commision number 2.1.1.297: peptide chain release factor N(5)-glutamine methyltransferase.
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 SAH A G117 T118 D140 R141 M142 D167 W168 N183 A206 G116 T117 D139 R140 M141 D166 W167 N182 A205
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0008168 methyltransferase activity
GO:0008170 N-methyltransferase activity
GO:0008276 protein methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0036009 protein-glutamine N-methyltransferase activity
GO:0102559 protein-(glutamine-N5) methyltransferase activity
Biological Process
GO:0006415 translational termination
GO:0006479 protein methylation
GO:0010468 regulation of gene expression
GO:0018364 peptidyl-glutamine methylation
GO:0032259 methylation
GO:0043414 macromolecule methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1t43, PDBe:1t43, PDBj:1t43
PDBsum1t43
PubMed15223314
UniProtP0ACC1|PRMC_ECOLI Release factor glutamine methyltransferase (Gene Name=prmC)

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