Structure of PDB 7mys Chain A

Receptor sequence
>7mysA (length=239) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
HVFFAVITLFPEMFDAITAYGISGRAAKRDIVQVTCINPRDFAEGNYRRV
DERPFGGGPGMVMMAEPLAKAINHAKQLASRAGCVHVPVVYMSPQGKTLN
EQAVQQFVDYDGLIVLCGRYEGVDERLIQHYVDQEWSIGDYVLSGGELPA
MVLLDSIIRRLPNVAIQDSFVDGLLDCPQYTKPDQFEGLDVPEILKSGHH
ANIEKWRFLQRYQRTLERRPELIEQVTLTKQQKKWLSDE
3D structure
PDB7mys Crystal structure of a tRNA (guanine-N1)-methyltransferase from Acinetobacter baumannii AB5075-UW bound to S-adenosyl homocysteine
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) P93 E120 R158 D173
Catalytic site (residue number reindexed from 1) P94 E121 R159 D168
Enzyme Commision number 2.1.1.228: tRNA (guanine(37)-N(1))-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 Y90 M91 S92 P93 G117 E120 I137 L142 G144 G145 P148 Y91 M92 S93 P94 G118 E121 I138 L143 G145 G146 P149
BS02 SAH A S174 D181 S169 D176
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0052906 tRNA (guanine(37)-N1)-methyltransferase activity
Biological Process
GO:0002939 tRNA N1-guanine methylation
GO:0006400 tRNA modification
GO:0008033 tRNA processing
GO:0032259 methylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7mys, PDBe:7mys, PDBj:7mys
PDBsum7mys
PubMed
UniProtB0V8J1|TRMD_ACIBY tRNA (guanine-N(1)-)-methyltransferase (Gene Name=trmD)

[Back to BioLiP]