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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
A0006672biological_processceramide metabolic process
A0006686biological_processsphingomyelin biosynthetic process
A0006940biological_processregulation of smooth muscle contraction
A0010508biological_processpositive regulation of autophagy
A0016020cellular_componentmembrane
A0017059cellular_componentserine palmitoyltransferase complex
A0030148biological_processsphingolipid biosynthetic process
A0030667cellular_componentsecretory granule membrane
A0035579cellular_componentspecific granule membrane
A0042552biological_processmyelination
A0044255biological_processcellular lipid metabolic process
A0061744biological_processmotor behavior
A0090153biological_processregulation of sphingolipid biosynthetic process
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
C0006665biological_processsphingolipid metabolic process
C0006686biological_processsphingomyelin biosynthetic process
C0009058biological_processbiosynthetic process
C0016020cellular_componentmembrane
C0016746molecular_functionacyltransferase activity
C0017059cellular_componentserine palmitoyltransferase complex
C0030148biological_processsphingolipid biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
C0046511biological_processsphinganine biosynthetic process
C0046512biological_processsphingosine biosynthetic process
C0046513biological_processceramide biosynthetic process
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
E0006665biological_processsphingolipid metabolic process
E0008104biological_processprotein localization
E0016020cellular_componentmembrane
E0017059cellular_componentserine palmitoyltransferase complex
E0030148biological_processsphingolipid biosynthetic process
E0046512biological_processsphingosine biosynthetic process
E0046513biological_processceramide biosynthetic process
S0004758molecular_functionserine C-palmitoyltransferase activity
S0005515molecular_functionprotein binding
S0005783cellular_componentendoplasmic reticulum
S0005789cellular_componentendoplasmic reticulum membrane
S0006665biological_processsphingolipid metabolic process
S0006686biological_processsphingomyelin biosynthetic process
S0009058biological_processbiosynthetic process
S0016020cellular_componentmembrane
S0016746molecular_functionacyltransferase activity
S0017059cellular_componentserine palmitoyltransferase complex
S0030148biological_processsphingolipid biosynthetic process
S0030170molecular_functionpyridoxal phosphate binding
S0046511biological_processsphinganine biosynthetic process
S0046512biological_processsphingosine biosynthetic process
S0046513biological_processceramide biosynthetic process
S1904504biological_processpositive regulation of lipophagy
S1904649biological_processregulation of fat cell apoptotic process
T0004758molecular_functionserine C-palmitoyltransferase activity
T0005515molecular_functionprotein binding
T0005783cellular_componentendoplasmic reticulum
T0005789cellular_componentendoplasmic reticulum membrane
T0006665biological_processsphingolipid metabolic process
T0006686biological_processsphingomyelin biosynthetic process
T0009058biological_processbiosynthetic process
T0016020cellular_componentmembrane
T0016740molecular_functiontransferase activity
T0016746molecular_functionacyltransferase activity
T0017059cellular_componentserine palmitoyltransferase complex
T0030148biological_processsphingolipid biosynthetic process
T0030170molecular_functionpyridoxal phosphate binding
T0046511biological_processsphinganine biosynthetic process
T0046512biological_processsphingosine biosynthetic process
T0046513biological_processceramide biosynthetic process
T0060612biological_processadipose tissue development
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 Residues69
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-GLY21
ALEU64-LYS100
APRO140-TYR153

site_idSWS_FT_FI2
Number of Residues73
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:33558762, ECO:0007744|PDB:6M4N, ECO:0007744|PDB:6M4O, ECO:0007744|PDB:7CQI, ECO:0007744|PDB:7CQK
ChainResidueDetails
AILE22-SER44
AVAL45-PHE63
APHE101-THR117
AILE122-LEU139

site_idSWS_FT_FI3
Number of Residues3
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
ALYS118-GLN121
CARG37-LEU473

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Hydroxyproline => ECO:0000269|PubMed:36408842
ChainResidueDetails
APRO137
CTYR164

222415

PDB entries from 2024-07-10

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