Structure of PDB 4yqo Chain A

Receptor sequence
>4yqoA (length=242) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
GLVPRGSHMWIGVISLFPEMFKAITEFGVTGRAVKHNLLKVECWNPRDFT
FDKHKTVDDRPYGGGPGMLMMVQPLRDAIHTAKAAAGEGAKVIYLSPQGR
KLDQGGVTELAQNQKLILVCGRYEGIDERLIQTEIDEEWSIGDYVLTGGE
LPAMTLIDAVARFIPGVLDGLLDCPHYTRPEVLEGLTVPPVLMSGHHEEI
RKWRLKQSLQRTWLRRPELLEGLALTDEQRKLLKEAQAEHNS
3D structure
PDB4yqo Crystal structure of TrmD, a M1G37 tRNA Methyltransferase with SAM-competitive compounds
ChainA
Resolution1.68 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) P89 E116 R154
Catalytic site (residue number reindexed from 1) P97 E124 R162
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 4H1 A L87 S88 P89 E116 S132 I133 Y136 L138 G140 P144 L95 S96 P97 E124 S140 I141 Y144 L146 G148 P152 BindingDB: IC50=501nM
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:4yqo, PDBe:4yqo, PDBj:4yqo
PDBsum4yqo
PubMed
UniProtP43912|TRMD_HAEIN tRNA (guanine-N(1)-)-methyltransferase (Gene Name=trmD)

[Back to BioLiP]