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6S7T

Cryo-EM structure of human oligosaccharyltransferase complex OST-B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004576molecular_functionoligosaccharyl transferase activity
A0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processprotein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0006516biological_processglycoprotein catabolic process
A0006986biological_processresponse to unfolded protein
A0008250cellular_componentoligosaccharyltransferase complex
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0018279biological_processprotein N-linked glycosylation via asparagine
A0032991cellular_componentprotein-containing complex
A0034998cellular_componentoligosaccharyltransferase I complex
A0036503biological_processERAD pathway
A0043686biological_processco-translational protein modification
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processprotein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0008250cellular_componentoligosaccharyltransferase complex
B0016020cellular_componentmembrane
B0018279biological_processprotein N-linked glycosylation via asparagine
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006486biological_processprotein glycosylation
C0006487biological_processprotein N-linked glycosylation
C0006954biological_processinflammatory response
C0008250cellular_componentoligosaccharyltransferase complex
C0016020cellular_componentmembrane
C0032991cellular_componentprotein-containing complex
C0034976biological_processresponse to endoplasmic reticulum stress
C0034998cellular_componentoligosaccharyltransferase I complex
C0043227cellular_componentmembrane-bounded organelle
C0062062molecular_functionoligosaccharyltransferase complex binding
C1904019biological_processepithelial cell apoptotic process
D0001824biological_processblastocyst development
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006486biological_processprotein glycosylation
D0006487biological_processprotein N-linked glycosylation
D0006915biological_processapoptotic process
D0008047molecular_functionenzyme activator activity
D0008250cellular_componentoligosaccharyltransferase complex
D0016020cellular_componentmembrane
D0018279biological_processprotein N-linked glycosylation via asparagine
D0031647biological_processregulation of protein stability
D0043066biological_processnegative regulation of apoptotic process
E0006486biological_processprotein glycosylation
E0016020cellular_componentmembrane
F0006487biological_processprotein N-linked glycosylation
F0008250cellular_componentoligosaccharyltransferase complex
F0016020cellular_componentmembrane
G0005789cellular_componentendoplasmic reticulum membrane
G0018279biological_processprotein N-linked glycosylation via asparagine
I0030246molecular_functioncarbohydrate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues384
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
GSER43-PRO427
HTHR231-HIS270
HARG322-SER335
AMET283-SER287
AASP342-GLN350
ALYS434-GLU439
ATYR483-LYS526

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
GTYR428-LEU447
HMET210-MET230
HILE271-THR291
HILE301-PHE321
AVAL246-VAL260
ATYR266-LEU282
ALYS288-PHE313
AMET322-ARG341
ATRP411-ILE433
AARG440-VAL456
AMET461-HIS482
ATHR527-VAL552

site_idSWS_FT_FI3
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
GHIS448-ASP456
HSER292-LYS300
ASER261-GLY265
AGLN314-HIS321
ATHR372-THR410
AMET457-LEU460
AHIS553-VAL826

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ITYR82
ITYR104
ITYR131
IPHE132
IASP201

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLU223
AARG459
ATYR609
IASN268
AASP221

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
ALYS674
EASN299
AGLU405

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ELYS538

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AALA2

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3TDQ1
ChainResidueDetails
ASER13

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER18

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER29

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER498

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER499

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN641
AASN616

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN623

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN627

221051

PDB entries from 2024-06-12

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