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3A2B

Crystal Structure of Serine Palmitoyltransferase from Sphingobacterium multivorum with substrate L-serine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004758molecular_functionserine C-palmitoyltransferase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006665biological_processsphingolipid metabolic process
A0008710molecular_function8-amino-7-oxononanoate synthase activity
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SER A 401
ChainResidue
AHIS138
ALYS244
APHE272
AALA274
APLP400
AHOH510
AHOH516
AHOH599

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP A 400
ChainResidue
AGLY113
APHE114
AHIS138
ASER140
AASP181
AASP210
AALA212
AHIS213
AMET239
ATHR241
ASER243
ALYS244
ASER273
AALA274
ASER401
AHOH501
AHOH524
ATHR112

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKSLASLG
ChainResidueDetails
ATHR241-GLY250

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19564159
ChainResidueDetails
AGLY113
AHIS213
ASER243

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q93UV0
ChainResidueDetails
ATHR241

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q93UV0
ChainResidueDetails
ALYS244

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
AHIS213
ALYS244

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
AHIS138
AASP210
ALYS244

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
AHIS138
AASP210

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
AARG82

223166

PDB entries from 2024-07-31

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