Structure of PDB 1vq1 Chain A

Receptor sequence
>1vq1A (length=266) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
RKIWSLIRDCSGKLEGVTETSVLEVLLIVSRVLGIRKEDLFLKDLGVSPT
EEKRILELVEKRASGYPLHYILGEKEFMGLSFLVEEGVFVPRPETEELVE
LALELIRKYGIKTVADIGTGSGAIGVSVAKFSDAIVFATDVSSKAVEIAR
KNAERHGVSDRFFVRKGEFLEPFKEKFASIEMILSNPPYVKSSAHLFEPP
EALFGGEDGLDFYREFFGRYDTSGKIVLMEIGEDQVEELKKIVSDTVFLK
DSAGKYRFLLLNRRSS
3D structure
PDB1vq1 Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution
ChainA
Resolution2.8 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) F89 N186 P187
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 SAM A F100 I128 G129 T130 G131 D151 E179 F180 N197 P198 P199 A218 F228 F89 I117 G118 T119 G120 D140 E168 F169 N186 P187 P188 A202 F212
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:1vq1, PDBe:1vq1, PDBj:1vq1
PDBsum1vq1
PubMed
UniProtQ9WYV8|PRMC_THEMA Release factor glutamine methyltransferase (Gene Name=prmC)

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