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4YQ5

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 Residues15
Detailsbinding site for residue 4G0 A 301
ChainResidue
ATYR86
ALEU138
AGLY140
AGLY141
APRO144
APHE171
AASP177
ALEU87
ASER88
AGLY113
AGLU116
ASER132
AILE133
AGLY134
ATYR136

site_idAC2
Number of Residues10
Detailsbinding site for residue FLC A 302
ChainResidue
AGLY20
AVAL21
AARG24
AARG114
ATYR115
ATHR230
AASP231
AARG234
AHOH419
AHOH425

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

227344

PDB entries from 2024-11-13

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