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7YJN

Cryo-EM structure of the monomeric atSPT-ORM1 (ORM1-N17A) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0004758molecular_functionserine C-palmitoyltransferase activity
B0005773cellular_componentvacuole
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006665biological_processsphingolipid metabolic process
B0006915biological_processapoptotic process
B0009058biological_processbiosynthetic process
B0009555biological_processpollen development
B0009640biological_processphotomorphogenesis
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0043067biological_processregulation of programmed cell death
B0046512biological_processsphingosine biosynthetic process
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0009555biological_processpollen development
C0016020cellular_componentmembrane
C0044877molecular_functionprotein-containing complex binding
C0090153biological_processregulation of sphingolipid biosynthetic process
C1904222biological_processpositive regulation of serine C-palmitoyltransferase activity
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006979biological_processresponse to oxidative stress
D0010150biological_processleaf senescence
D0016020cellular_componentmembrane
D0030148biological_processsphingolipid biosynthetic process
D0034976biological_processresponse to endoplasmic reticulum stress
D0042742biological_processdefense response to bacterium
D0090156biological_processintracellular sphingolipid homeostasis
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 Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
EVAL32-LEU52

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
BLYS311

221716

PDB entries from 2024-06-26

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