Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1P0Y

Crystal structure of the SET domain of LSMT bound to MeLysine 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 Residues19
DetailsBINDING SITE FOR RESIDUE SAH A 800
ChainResidue
AGLU80
ATYR300
AGLY301
APHE302
AHOH803
AHOH825
AHOH858
AHOH867
AHOH982
AHOH997
CMLZ900
AGLY81
ALEU82
ASER221
AARG222
AASP239
AASN242
AHIS243
ATYR287

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH B 801
ChainResidue
BGLU80
BLEU82
BSER221
BARG222
BASP239
BLEU240
BILE241
BASN242
BHIS243
BTYR287
BTYR300
BGLY301
BPHE302
BHOH802
BHOH804
BHOH811
BHOH908
BHOH909
CPHE263
CHOH935

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH C 802
ChainResidue
CGLU80
CLEU82
CSER221
CARG222
CASP239
CLEU240
CASN242
CHIS243
CTYR287
CTYR300
CGLY301
CPHE302
CMLZ902
CHOH904
CHOH909
CHOH954
CHOH1097

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MLZ C 900
ChainResidue
AARG222
APHE224
ASER225
AARG226
AASP239
ATYR254
ATYR287
ATYR300
ASAH800
AHOH990
CHOH996

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLZ C 901
ChainResidue
BARG222
BPHE224
BSER225
BARG226
BASP239
BILE241
BHIS252
BTYR287
CHOH906
CHOH916

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MLZ C 902
ChainResidue
CSER221
CARG222
CALA223
CPHE224
CSER225
CARG226
CASP239
CILE241
CTYR254
CTYR287
CLYS291
CTYR300
CSAH802
CHOH1062
CHOH1067

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon