Structure of PDB 1nv9 Chain A

Receptor sequence
>1nv9A (length=264) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KIWSLIRDCSGKLEGVTETSVLEVLLIVSRVLGIRKEDLFLKDLGVSPTE
EKRILELVEKRASGYPLHYILGEKEFMGLSFLVEEGVFVPRPETEELVEL
ALELIRKYGIKTVADIGTGSGAIGVSVAKFSDAIVFATDVSSKAVEIARK
NAERHGVSDRFFVRKGEFLEPFKEKFASIEMILSNPPYVKSSALFEPPEA
LFGGEDGLDFYREFFGRYDTSGKIVLMEIGEDQVEELKKIVSDTVFLKDS
AGKYRFLLLNRRSS
3D structure
PDB1nv9 Structures along the Catalytic Pathway of PrmC/HemK, an N(5)-Glutamine AdoMet-Dependent Methyltransferase
ChainA
Resolution2.356 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F100 N197 P198
Catalytic site (residue number reindexed from 1) F88 N185 P186
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 F100 G129 T130 G131 D151 E179 F180 N197 P199 A218 F88 G117 T118 G119 D139 E167 F168 N185 P187 A200
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:0006479 protein methylation
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:1nv9, PDBe:1nv9, PDBj:1nv9
PDBsum1nv9
PubMed12741815
UniProtQ9WYV8|PRMC_THEMA Release factor glutamine methyltransferase (Gene Name=prmC)

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