Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7CQI

Cryo-EM structure of the substrate-bound SPT-ORMDL3 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0002903biological_processnegative regulation of B cell apoptotic process
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006665biological_processsphingolipid metabolic process
A0006672biological_processceramide metabolic process
A0010508biological_processpositive regulation of autophagy
A0016020cellular_componentmembrane
A0017059cellular_componentserine palmitoyltransferase complex
A0030148biological_processsphingolipid biosynthetic process
A0030667cellular_componentsecretory granule membrane
A0035579cellular_componentspecific granule membrane
A0090156biological_processintracellular sphingolipid homeostasis
A1900060biological_processnegative regulation of ceramide biosynthetic process
A1900182biological_processpositive regulation of protein localization to nucleus
A2000303biological_processregulation of ceramide biosynthetic process
C0004758molecular_functionserine C-palmitoyltransferase activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006629biological_processlipid metabolic process
C0006665biological_processsphingolipid metabolic process
C0006686biological_processsphingomyelin biosynthetic process
C0006688biological_processglycosphingolipid biosynthetic process
C0009058biological_processbiosynthetic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0017059cellular_componentserine palmitoyltransferase complex
C0030148biological_processsphingolipid biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
C0043604biological_processamide biosynthetic process
C0046512biological_processsphingosine biosynthetic process
C0046513biological_processceramide biosynthetic process
C0098554cellular_componentcytoplasmic side of endoplasmic reticulum membrane
C1904504biological_processpositive regulation of lipophagy
C1904649biological_processregulation of fat cell apoptotic process
E0004758molecular_functionserine C-palmitoyltransferase activity
E0005515molecular_functionprotein binding
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0006629biological_processlipid metabolic process
E0006665biological_processsphingolipid metabolic process
E0006686biological_processsphingomyelin biosynthetic process
E0006688biological_processglycosphingolipid biosynthetic process
E0008104biological_processintracellular protein localization
E0017059cellular_componentserine palmitoyltransferase complex
E0030148biological_processsphingolipid biosynthetic process
E0046512biological_processsphingosine biosynthetic process
E0046513biological_processceramide biosynthetic process
E0098554cellular_componentcytoplasmic side of endoplasmic reticulum membrane
S0004758molecular_functionserine C-palmitoyltransferase activity
S0005515molecular_functionprotein binding
S0005783cellular_componentendoplasmic reticulum
S0005789cellular_componentendoplasmic reticulum membrane
S0006629biological_processlipid metabolic process
S0006665biological_processsphingolipid metabolic process
S0006686biological_processsphingomyelin biosynthetic process
S0006688biological_processglycosphingolipid biosynthetic process
S0009058biological_processbiosynthetic process
S0016740molecular_functiontransferase activity
S0016746molecular_functionacyltransferase activity
S0017059cellular_componentserine palmitoyltransferase complex
S0030148biological_processsphingolipid biosynthetic process
S0030170molecular_functionpyridoxal phosphate binding
S0043604biological_processamide biosynthetic process
S0046512biological_processsphingosine biosynthetic process
S0046513biological_processceramide biosynthetic process
S0098554cellular_componentcytoplasmic side of endoplasmic reticulum membrane
S1904504biological_processpositive regulation of lipophagy
S1904649biological_processregulation of fat cell apoptotic process
T0004758molecular_functionserine C-palmitoyltransferase activity
T0005515molecular_functionprotein binding
T0005789cellular_componentendoplasmic reticulum membrane
T0006629biological_processlipid metabolic process
T0006665biological_processsphingolipid metabolic process
T0006686biological_processsphingomyelin biosynthetic process
T0006688biological_processglycosphingolipid biosynthetic process
T0009058biological_processbiosynthetic process
T0016740molecular_functiontransferase activity
T0016746molecular_functionacyltransferase activity
T0017059cellular_componentserine palmitoyltransferase complex
T0030148biological_processsphingolipid biosynthetic process
T0030170molecular_functionpyridoxal phosphate binding
T0046512biological_processsphingosine biosynthetic process
T0046513biological_processceramide biosynthetic process
T0060612biological_processadipose tissue development
T0098554cellular_componentcytoplasmic side of endoplasmic reticulum membrane
T1904504biological_processpositive regulation of lipophagy
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue PLS T 601
ChainResidue
SPRO135
THIS347
TMET374
TTHR376
TTHR378
TLYS379
TGE0602
SSER338
SALA339
TTYR176
TGLY238
TASN242
THIS263
TGLU315
TASP344

site_idAC2
Number of Residues20
Detailsbinding site for residue GE0 T 602
ChainResidue
AASP76
SPRO135
SPHE138
SARG181
SARG203
SCYS336
TTYR122
TTRP134
TSER258
TASP259
TGLU260
TASN262
THIS263
TVAL267
TARG271
TILE279
TSER319
TGLY497
TPRO499
TPLS601

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFTKSFGASG
ChainResidueDetails
TTHR376-GLY385

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL","evidences":[{"source":"PubMed","id":"23629659","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues73
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33558762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6M4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CQI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CQK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues36
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues7
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Hydroxyproline","evidences":[{"source":"PubMed","id":"36408842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Within the serine palmitoyltransferase (SPT) complex, defines the length of the acyl chain-binding pocket, determining the acyl-CoA substrate preference"}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon