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1OZV

Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy

Functional Information from GO Data
ChainGOidnamespacecontents
A0009507cellular_componentchloroplast
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0018022biological_processpeptidyl-lysine methylation
A0030785molecular_function[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity
B0009507cellular_componentchloroplast
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0018022biological_processpeptidyl-lysine methylation
B0030785molecular_function[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity
C0009507cellular_componentchloroplast
C0016279molecular_functionprotein-lysine N-methyltransferase activity
C0018022biological_processpeptidyl-lysine methylation
C0030785molecular_function[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LYS A 700
ChainResidue
ASER221
ATYR300
ASAH1000
AARG222
AALA223
ASER225
AARG226
AASP239
AILE241
ATYR254
ATYR287

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LYS A 800
ChainResidue
AHOH1002
AHOH1023
BSER221
BARG222
BPHE224
BSER225
BTYR287

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LYS A 900
ChainResidue
AHOH1003
AHOH1036
CSER221
CARG222
CPHE224
CSER225
CARG226
CASP239
CTYR254
CTYR287
CTYR300
CSAH1002

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAH A 1000
ChainResidue
AGLU80
AGLY81
ALEU82
APRO151
ASER221
AARG222
AASP239
AASN242
AHIS243
ATYR287
ATYR300
ALYS700
AHOH1006
AHOH1035
AHOH1067
AHOH1071
AHOH1099
AHOH1105

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH B 1001
ChainResidue
BGLU80
BGLY81
BLEU82
BSER221
BARG222
BASP239
BASN242
BHIS243
BTYR287
BTYR300
BPHE302
BHOH1006
BHOH1012
BHOH1013
BHOH1021
BHOH1176
CPHE263

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAH C 1002
ChainResidue
ALYS900
CGLU80
CLEU82
CSER221
CARG222
CASP239
CLEU240
CILE241
CASN242
CHIS243
CTYR287
CTYR300
CGLY301
CPHE302
CHOH1013
CHOH1039

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLU80
AASN242
BGLU80
BASN242
CGLU80
CASN242

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:12819771, ECO:0000269|PubMed:16682405
ChainResidueDetails
AARG222
BTYR254
BTYR287
BTYR300
CARG222
CARG226
CASP239
CTYR254
CTYR287
CTYR300
AARG226
AASP239
ATYR254
ATYR287
ATYR300
BARG222
BARG226
BASP239

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mlv
ChainResidueDetails
ATYR287

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mlv
ChainResidueDetails
BTYR287

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mlv
ChainResidueDetails
CTYR287

site_idMCSA1
Number of Residues1
DetailsM-CSA 604
ChainResidueDetails
ATYR287activator, proton acceptor, proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 604
ChainResidueDetails
BTYR287activator, proton acceptor, proton donor

site_idMCSA3
Number of Residues1
DetailsM-CSA 604
ChainResidueDetails
CTYR287activator, proton acceptor, proton donor

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PDB entries from 2024-08-28

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