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4YQC

Crystal structure of TrmD, a M1G37 tRNA Methyltransferase with SAM-competitive compounds

Functional Information from GO Data
ChainGOidnamespacecontents
A0002939biological_processtRNA N1-guanine methylation
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
A0052906molecular_functiontRNA (guanine(37)-N1)-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue EFW A 301
ChainResidue
ATYR86
AGLY134
ATYR136
ALEU138
APRO144
AHOH415
ALEU87
ASER88
APRO89
AGLY113
ATYR115
AGLY117
ASER132
AILE133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
AASP169

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATYR86
AGLY113
AILE133

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 332
ChainResidueDetails
APRO89increase nucleophilicity, steric role
AGLU116electrostatic stabiliser, hydrogen bond acceptor
AARG154activator, electrostatic stabiliser, hydrogen bond donor
AASP169activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor

226707

PDB entries from 2024-10-30

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