6S7T
Cryo-EM structure of human oligosaccharyltransferase complex OST-B
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004576 | molecular_function | oligosaccharyl transferase activity |
A | 0004579 | molecular_function | dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006486 | biological_process | protein glycosylation |
A | 0006487 | biological_process | protein N-linked glycosylation |
A | 0006516 | biological_process | glycoprotein catabolic process |
A | 0006986 | biological_process | response to unfolded protein |
A | 0008250 | cellular_component | oligosaccharyltransferase complex |
A | 0016020 | cellular_component | membrane |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034998 | cellular_component | oligosaccharyltransferase I complex |
A | 0036503 | biological_process | ERAD pathway |
A | 0043686 | biological_process | co-translational protein modification |
A | 0043687 | biological_process | post-translational protein modification |
A | 0046872 | molecular_function | metal ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006486 | biological_process | protein glycosylation |
B | 0006487 | biological_process | protein N-linked glycosylation |
B | 0008250 | cellular_component | oligosaccharyltransferase complex |
B | 0016020 | cellular_component | membrane |
B | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005789 | cellular_component | endoplasmic reticulum membrane |
C | 0006486 | biological_process | protein glycosylation |
C | 0006487 | biological_process | protein N-linked glycosylation |
C | 0006954 | biological_process | inflammatory response |
C | 0008250 | cellular_component | oligosaccharyltransferase complex |
C | 0016020 | cellular_component | membrane |
C | 0032991 | cellular_component | protein-containing complex |
C | 0034976 | biological_process | response to endoplasmic reticulum stress |
C | 0034998 | cellular_component | oligosaccharyltransferase I complex |
C | 0043227 | cellular_component | membrane-bounded organelle |
C | 0062062 | molecular_function | oligosaccharyltransferase complex binding |
C | 1904019 | biological_process | epithelial cell apoptotic process |
D | 0001824 | biological_process | blastocyst development |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0005789 | cellular_component | endoplasmic reticulum membrane |
D | 0006486 | biological_process | protein glycosylation |
D | 0006487 | biological_process | protein N-linked glycosylation |
D | 0006915 | biological_process | apoptotic process |
D | 0008047 | molecular_function | enzyme activator activity |
D | 0008250 | cellular_component | oligosaccharyltransferase complex |
D | 0016020 | cellular_component | membrane |
D | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
D | 0031647 | biological_process | regulation of protein stability |
D | 0043066 | biological_process | negative regulation of apoptotic process |
E | 0006486 | biological_process | protein glycosylation |
E | 0016020 | cellular_component | membrane |
F | 0006487 | biological_process | protein N-linked glycosylation |
F | 0008250 | cellular_component | oligosaccharyltransferase complex |
F | 0016020 | cellular_component | membrane |
G | 0005789 | cellular_component | endoplasmic reticulum membrane |
G | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
I | 0030246 | molecular_function | carbohydrate binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 384 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
G | SER43-PRO427 | |
H | THR231-HIS270 | |
H | ARG322-SER335 | |
A | MET283-SER287 | |
A | ASP342-GLN350 | |
A | LYS434-GLU439 | |
A | TYR483-LYS526 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
G | TYR428-LEU447 | |
H | MET210-MET230 | |
H | ILE271-THR291 | |
H | ILE301-PHE321 | |
A | VAL246-VAL260 | |
A | TYR266-LEU282 | |
A | LYS288-PHE313 | |
A | MET322-ARG341 | |
A | TRP411-ILE433 | |
A | ARG440-VAL456 | |
A | MET461-HIS482 | |
A | THR527-VAL552 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
G | HIS448-ASP456 | |
H | SER292-LYS300 | |
A | SER261-GLY265 | |
A | GLN314-HIS321 | |
A | THR372-THR410 | |
A | MET457-LEU460 | |
A | HIS553-VAL826 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
I | TYR82 | |
I | TYR104 | |
I | TYR131 | |
I | PHE132 | |
I | ASP201 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | GLU223 | |
A | ARG459 | |
A | TYR609 | |
I | ASN268 | |
A | ASP221 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | LYS674 | |
E | ASN299 | |
A | GLU405 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211 |
Chain | Residue | Details |
E | LYS538 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3TDQ1 |
Chain | Residue | Details |
A | SER13 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER18 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER29 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER498 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER499 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN641 | |
A | ASN616 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN623 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN627 |