Structure of PDB 2b3t Chain A

Receptor sequence
>2b3tA (length=276) Species: 562 (Escherichia coli) [Search protein sequence]
MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDE
QCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVE
QALARLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQ
RNAQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR
FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAF
ILAGYHDVETCRDYGDNERVTLGRYY
3D structure
PDB2b3t Molecular basis for bacterial class I release factor methylation by PrmC
ChainA
Resolution3.1 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) L89 N183 P184
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 T88 L89 P91 G117 T120 D140 R141 S166 D167 W168 N183 P185 T205 A206 T88 L89 P91 G117 T120 D140 R141 S166 D167 W168 N183 P185 T205 A206
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:2b3t, PDBe:2b3t, PDBj:2b3t
PDBsum2b3t
PubMed16364916
UniProtP0ACC1|PRMC_ECOLI Release factor glutamine methyltransferase (Gene Name=prmC)

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