Structure of PDB 2jjq Chain A

Receptor sequence
>2jjqA (length=392) Species: 29292 (Pyrococcus abyssi) [Search protein sequence]
MRGVIRKLNDDGFGVLKGILVPFSAPGDEIIVERVERVKKRRVASQWKLV
RSSPLRVGCTLQHLNYDYQLEFKRKKLKRILGFEVEVVPSPKIFGHRNRI
DLAITKDGIGFREKWWKIVDIDECPVFGKTSREAIERLKEFIEEEKISVW
NIKKDEGFLRYMVLREGKFTEEVMVNFVTKEGNLPDPTNYFDFDSIYWSV
NRSKSDVSYGDIERFWGKEFIRERLDDVDYLIHPNSFFQTNSYQAVNLVR
KVSELVEGEKILDMYSGVGTFGIYLAKRGFNVKGFDSNEFAIEMARRNVE
INNVDAEFEVASDREVSVKGFDTVIVDPPRAGLHPRLVKRLNREKPGVIV
YVSCNPETFARDVKMLDYRIDEIVALDMFPHTPHVELVAKLV
3D structure
PDB2jjq The Crystal Structure of Pyrococcus Abyssi tRNA (Uracil-54, C5)-Methyltransferase Provides Insights Into its tRNA Specificity.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A25
Catalytic site (residue number reindexed from 1) A25
Enzyme Commision number 2.1.1.35: tRNA (uracil(54)-C(5))-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 Q252 Y278 S279 T283 D299 S300 S325 D326 D340 P342 Q239 Y265 S266 T270 D286 S287 S312 D313 D327 P329
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008173 RNA methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0030697 tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006396 RNA processing
GO:0008033 tRNA processing
GO:0009451 RNA modification
GO:0030488 tRNA methylation
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2jjq, PDBe:2jjq, PDBj:2jjq
PDBsum2jjq
PubMed18653523
UniProtQ9UZR7|ATRMA_PYRAB tRNA (uracil(54)-C(5))-methyltransferase (Gene Name=PYRAB10780)

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