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1UAM

Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
APHE9
AGLY20
AVAL21
AARG24
AARG114
ATYR115

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SAH A 301
ChainResidue
APRO89
AGLN90
AGLY113
ATYR115
AGLU116
AGLY117
ASER132
AILE133
AGLY134
ATYR136
AVAL137
ALEU138
ATHR139
AGLY140
AGLY141
APRO144
AASP169
ASER170
AASP177
AHOH1032
ATYR86
ALEU87
ASER88

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
AASP169activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor
APRO89increase nucleophilicity, steric role
AGLU116electrostatic stabiliser, hydrogen bond acceptor
AARG154activator, electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-29

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