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5TWK

Crystal Structure of RlmH in Complex with Sinefungin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A0042803molecular_functionprotein homodimerization activity
A0043022molecular_functionribosome binding
A0070038molecular_functionrRNA (pseudouridine-N3-)-methyltransferase activity
A0070475biological_processrRNA base methylation
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0008168molecular_functionmethyltransferase activity
B0031167biological_processrRNA methylation
B0032259biological_processmethylation
B0042803molecular_functionprotein homodimerization activity
B0043022molecular_functionribosome binding
B0070038molecular_functionrRNA (pseudouridine-N3-)-methyltransferase activity
B0070475biological_processrRNA base methylation
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006364biological_processrRNA processing
C0008168molecular_functionmethyltransferase activity
C0031167biological_processrRNA methylation
C0032259biological_processmethylation
C0042803molecular_functionprotein homodimerization activity
C0043022molecular_functionribosome binding
C0070038molecular_functionrRNA (pseudouridine-N3-)-methyltransferase activity
C0070475biological_processrRNA base methylation
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006364biological_processrRNA processing
D0008168molecular_functionmethyltransferase activity
D0031167biological_processrRNA methylation
D0032259biological_processmethylation
D0042803molecular_functionprotein homodimerization activity
D0043022molecular_functionribosome binding
D0070038molecular_functionrRNA (pseudouridine-N3-)-methyltransferase activity
D0070475biological_processrRNA base methylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue SFG C 201
ChainResidue
CLEU72
CSER123
CLEU125
CTHR126
CLEU127
CVAL132
CHOH307
DGLU155
CASP73
CILE74
CGLY103
CGLY104
CGLY107
CLEU108
CTRP120
CLEU122

site_idAC2
Number of Residues16
Detailsbinding site for residue SFG D 201
ChainResidue
CARG142
CGLU155
DLEU72
DASP73
DILE74
DGLY103
DGLY104
DPRO105
DGLY107
DLEU122
DSER123
DLEU125
DTHR126
DLEU127
DHIS129
DHOH337

site_idAC3
Number of Residues18
Detailsbinding site for residue SFG A 201
ChainResidue
ALEU72
AASP73
AILE74
AGLY103
AGLY104
APRO105
AGLU106
AGLY107
ALEU108
ATRP120
ALEU122
ASER123
ALEU125
ATHR126
ALEU127
AHOH313
BGLU155
BHOH317

site_idAC4
Number of Residues17
Detailsbinding site for residue SFG B 201
ChainResidue
AHOH301
BLEU72
BASP73
BILE74
BILE102
BGLY103
BGLY104
BPRO105
BGLY107
BLEU108
BTRP120
BLEU122
BSER123
BLEU125
BLEU127
BVAL132
BHOH306

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00658, ECO:0000269|PubMed:28428565, ECO:0007744|PDB:5TWJ
ChainResidueDetails
CLEU72
BLEU72
BGLY103
BLEU122
CGLY103
CLEU122
DLEU72
DGLY103
DLEU122
ALEU72
AGLY103
ALEU122

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PDB entries from 2024-07-17

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