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3LHD

Crystal structure of P. abyssi tRNA m1A58 methyltransferase in complex with S-adenosyl-L-homocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase activity
A0030488biological_processtRNA methylation
A0031515cellular_componenttRNA (m1A) methyltransferase complex
A0032259biological_processmethylation
A0043827molecular_functiontRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity
A0160107molecular_functiontRNA (adenine(58)-N1)-methyltransferase activity
B0008033biological_processtRNA processing
B0008168molecular_functionmethyltransferase activity
B0016740molecular_functiontransferase activity
B0030488biological_processtRNA methylation
B0031515cellular_componenttRNA (m1A) methyltransferase complex
B0032259biological_processmethylation
B0043827molecular_functiontRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity
B0160107molecular_functiontRNA (adenine(58)-N1)-methyltransferase activity
C0008033biological_processtRNA processing
C0008168molecular_functionmethyltransferase activity
C0016740molecular_functiontransferase activity
C0030488biological_processtRNA methylation
C0031515cellular_componenttRNA (m1A) methyltransferase complex
C0032259biological_processmethylation
C0043827molecular_functiontRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity
C0160107molecular_functiontRNA (adenine(58)-N1)-methyltransferase activity
D0008033biological_processtRNA processing
D0008168molecular_functionmethyltransferase activity
D0016740molecular_functiontransferase activity
D0030488biological_processtRNA methylation
D0031515cellular_componenttRNA (m1A) methyltransferase complex
D0032259biological_processmethylation
D0043827molecular_functiontRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity
D0160107molecular_functiontRNA (adenine(58)-N1)-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SAH C 301
ChainResidue
CGLY101
CPRO195
CHOH276
CGLY103
CGLU125
CILE126
CPHE130
CLYS152
CASP153
CILE154
CTYR155

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SAH A 301
ChainResidue
AGLY101
AGLY103
AGLU125
AILE126
APHE130
AASP153
AILE154
ATYR155
AASP169
APRO171

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SAH B 301
ChainResidue
BGLY101
BGLY103
BGLU125
BILE126
BPHE130
BLYS152
BASP153
BILE154
BTYR155
BASP169
BLEU170
BHOH271
BHOH277

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAH D 301
ChainResidue
DGLY101
DGLY103
DGLU125
DILE126
DARG127
DPHE130
DASP153
DILE154
DTYR155
DASP169
DLEU170
DPRO171
DPRO195
DGLN199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
CSER104
ASER104
BSER104
DSER104

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00952, ECO:0000269|PubMed:20483913
ChainResidueDetails
CGLU125
DGLU125
DASP153
DASP169
CASP153
CASP169
AGLU125
AASP153
AASP169
BGLU125
BASP153
BASP169

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PDB entries from 2024-10-30

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