Structure of PDB 1sg9 Chain B

Receptor sequence
>1sg9B (length=274) Species: 2336 (Thermotoga maritima) [Search protein sequence]
SGAERKIWSLIRDCSGKLEGVTETSVLEVLLIVSRVLGIRKEDLFLKDLG
VSPTEEKRILELVEKRASGYPLHYILGEKEFMGLSFLVEEGVFVPRPETE
ELVELALELIRKYGIKTVADIGTGSGAIGVSVAKFSDAIVFATDVSSKAV
EIARKNAERHGVSDRFFVRKGEFLEPFKEKFASIEMILSNPPYVKSSAHL
PKDVLFEPPEALFGGEDGLDFYREFFGRYDTSGKIVLMEIGEDQVEELKK
IVSDTVFLKDSAGKYRFLLLNRRS
3D structure
PDB1sg9 A novel mode of dimerization via formation of a glutamate anhydride crosslink in a protein crystal structure.
ChainB
Resolution2.3 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) F93 N190 P191
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 B F100 G129 T130 I135 D151 V152 E179 F180 N197 A218 F93 G122 T123 I128 D144 V145 E172 F173 N190 A211
BS02 GLN B F100 R103 N197 P198 Y200 F93 R96 N190 P191 Y193
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:1sg9, PDBe:1sg9, PDBj:1sg9
PDBsum1sg9
PubMed18247349
UniProtQ9WYV8|PRMC_THEMA Release factor glutamine methyltransferase (Gene Name=prmC)

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