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7YJK

Cryo-EM structure of the dimeric atSPT-ORM1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004758molecular_functionserine C-palmitoyltransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006665biological_processsphingolipid metabolic process
A0009058biological_processbiosynthetic process
A0009507cellular_componentchloroplast
A0009793biological_processembryo development ending in seed dormancy
A0009825biological_processmultidimensional cell growth
A0030148biological_processsphingolipid biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0043067biological_processregulation of programmed cell death
A0046512biological_processsphingosine biosynthetic process
A0046513biological_processceramide biosynthetic process
B0004758molecular_functionserine C-palmitoyltransferase activity
B0005773cellular_componentvacuole
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006665biological_processsphingolipid metabolic process
B0009058biological_processbiosynthetic process
B0009507cellular_componentchloroplast
B0009555biological_processpollen development
B0009640biological_processphotomorphogenesis
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0017059cellular_componentserine palmitoyltransferase complex
B0030170molecular_functionpyridoxal phosphate binding
B0043067biological_processregulation of programmed cell death
B0046512biological_processsphingosine biosynthetic process
B0046513biological_processceramide biosynthetic process
C0005789cellular_componentendoplasmic reticulum membrane
D0005789cellular_componentendoplasmic reticulum membrane
D0006672biological_processceramide metabolic process
D0016020cellular_componentmembrane
D0017059cellular_componentserine palmitoyltransferase complex
E0004758molecular_functionserine C-palmitoyltransferase activity
E0005515molecular_functionprotein binding
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0006665biological_processsphingolipid metabolic process
E0009058biological_processbiosynthetic process
E0009507cellular_componentchloroplast
E0009793biological_processembryo development ending in seed dormancy
E0009825biological_processmultidimensional cell growth
E0030148biological_processsphingolipid biosynthetic process
E0030170molecular_functionpyridoxal phosphate binding
E0043067biological_processregulation of programmed cell death
E0046512biological_processsphingosine biosynthetic process
E0046513biological_processceramide biosynthetic process
F0004758molecular_functionserine C-palmitoyltransferase activity
F0005773cellular_componentvacuole
F0005783cellular_componentendoplasmic reticulum
F0005789cellular_componentendoplasmic reticulum membrane
F0006665biological_processsphingolipid metabolic process
F0009058biological_processbiosynthetic process
F0009507cellular_componentchloroplast
F0009555biological_processpollen development
F0009640biological_processphotomorphogenesis
F0016020cellular_componentmembrane
F0016740molecular_functiontransferase activity
F0017059cellular_componentserine palmitoyltransferase complex
F0030170molecular_functionpyridoxal phosphate binding
F0043067biological_processregulation of programmed cell death
F0046512biological_processsphingosine biosynthetic process
F0046513biological_processceramide biosynthetic process
G0005789cellular_componentendoplasmic reticulum membrane
H0005789cellular_componentendoplasmic reticulum membrane
H0006672biological_processceramide metabolic process
H0016020cellular_componentmembrane
H0017059cellular_componentserine palmitoyltransferase complex
Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFTKSFGSCG
ChainResidueDetails
BTHR308-GLY317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

254917

PDB entries from 2026-06-10

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