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2JGT

Low resolution structure of SPT

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006665biological_processsphingolipid metabolic process
A0009058biological_processbiosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006665biological_processsphingolipid metabolic process
B0009058biological_processbiosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKSVGTVG
ChainResidueDetails
ATHR262-GLY271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17559874, ECO:0000269|PubMed:19376777, ECO:0007744|PDB:2JG2, ECO:0007744|PDB:2W8T, ECO:0007744|PDB:2W8U, ECO:0007744|PDB:2W8V
ChainResidueDetails
AGLY134
ATHR262
ASER264
BGLY134
BTHR262
BSER264

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17559874, ECO:0007744|PDB:2JG2
ChainResidueDetails
AHIS234
BHIS234

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17559874, ECO:0000269|PubMed:19376777, ECO:0007744|PDB:2JG2, ECO:0007744|PDB:2W8T, ECO:0007744|PDB:2W8U, ECO:0007744|PDB:2W8V
ChainResidueDetails
ALYS265
BLYS265

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
AASP231
AHIS159

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BHIS234
BLYS265

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
AARG103

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BARG103

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BASN106

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
AASP231
ALYS265
AHIS159
AGLU202

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BASP231
BLYS265
BGLU202

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
AASP231
ALYS265
AHIS159

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BASP231
BLYS265

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
ATYR135
AASP231
ALYS265

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
BTYR135
BASP231
BLYS265

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bs0
ChainResidueDetails
AHIS234
ALYS265

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PDB entries from 2025-06-18

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