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1M6Y

Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
A0070475biological_processrRNA base methylation
A0071424molecular_functionrRNA (cytosine-N4-)-methyltransferase activity
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0008168molecular_functionmethyltransferase activity
B0032259biological_processmethylation
B0070475biological_processrRNA base methylation
B0071424molecular_functionrRNA (cytosine-N4-)-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
AARG199
ALYS200
AARG201
AHOH556
AHOH600

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG199
BLYS200
BARG201
BHOH507

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 401
ChainResidue
AHIS8
ACYS31
ATHR32
AVAL33
AGLY34
AGLU35
AGLY36
AGLY37
AHIS38
AASP55
AVAL56
ASER81
ATYR82
AASP103
AGLY105
AGLN110
AMSE130
AASN221
AHOH508
AHOH524
AHOH563

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH B 402
ChainResidue
BHIS8
BCYS31
BTHR32
BVAL33
BGLY34
BGLU35
BGLY36
BGLY37
BHIS38
BASP55
BVAL56
BVAL60
BVAL80
BSER81
BTYR82
BASP103
BGLY105
BSER107
BGLN110
BMSE130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:12824489
ChainResidueDetails
BASP55
BTYR82
BASP103
BGLN110
AGLY36
AASP55
ATYR82
AASP103
AGLN110
BGLY36

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PDB entries from 2024-06-12

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