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2H23

Structure of Rubisco LSMT bound to Trimethyllysine 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 Residues17
DetailsBINDING SITE FOR RESIDUE SAH A 800
ChainResidue
AGLU80
ATYR287
ATYR300
AGLY301
APHE302
AM3L501
AHOH804
AHOH862
AHOH876
AGLY81
ALEU82
APRO151
ASER221
AARG222
AASP239
AASN242
AHIS243

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH B 801
ChainResidue
BGLU80
BGLY81
BLEU82
BPRO151
BSER221
BARG222
BASP239
BLEU240
BILE241
BASN242
BHIS243
BTYR287
BTYR300
BPHE302
BM3L502
BHOH804
BHOH811
BHOH829
BHOH887
BHOH905

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAH C 802
ChainResidue
CGLU80
CGLY81
CLEU82
CSER221
CARG222
CASP239
CASN242
CHIS243
CTYR287
CTYR300
CGLY301
CPHE302
CM3L500
CHOH823
CHOH894
CHOH898

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE M3L C 500
ChainResidue
CSER221
CARG222
CPHE224
CSER225
CARG226
CILE241
CTYR254
CTYR287
CTYR300
CSAH802

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE M3L A 501
ChainResidue
ASER221
AARG222
AALA223
APHE224
ASER225
AARG226
AILE241
ATYR287
ATYR300
ASAH800

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M3L B 502
ChainResidue
BSER221
BARG222
BPHE224
BSER225
BARG226
BASP239
BILE241
BHIS252
BTYR287
BSAH801
BHOH895

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 2024-10-09

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