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5OGL

Structure of bacterial oligosaccharyltransferase PglB in complex with an acceptor peptide and an lipid-linked oligosaccharide analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004576molecular_functionoligosaccharyl transferase activity
A0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
A0005886cellular_componentplasma membrane
A0006486biological_processprotein glycosylation
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0018279biological_processprotein N-linked glycosylation via asparagine
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 801
ChainResidue
AASP56
AASP154
AGLU319
AHOH902
AHOH903
AHOH910

site_idAC2
Number of Residues5
Detailsbinding site for residue MN A 802
ChainResidue
AASP475
AHOH906
AARG65
AGLN73
AASP76

site_idAC3
Number of Residues11
Detailsbinding site for residue 9UB A 803
ChainResidue
AASP56
ATYR79
ATYR196
ASER198
AGLN289
ATYR293
AMET368
AARG375
APHE376
ATYR379
ATYR468

site_idAC4
Number of Residues1
Detailsbinding site for residue NA A 804
ChainResidue
AGLU43

site_idAC5
Number of Residues7
Detailsbinding site for Ligand residues PPN B 16 through GLY B 17 bound to THR B 15
ChainResidue
AGLU315
ATHR316
AILE317
AMET318
AASN321
AVAL575
BTHR15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:21677752
ChainResidueDetails
AMET1-SER12
ATYR125-LEU127
ALYS177-ASP178
AHIS218-LYS222
ALYS257-ASN262
ALYS351-SER355
AGLU400-SER407

site_idSWS_FT_FI2
Number of Residues249
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:21677752
ChainResidueDetails
AILE13-TRP37
APHE99-GLU124
ATHR128-ASN146
ATHR155-ASN176
AILE179-TRP194
ATYR200-PHE217
AILE223-LEU235
ATRP240-PHE256
APHE263-SER280
APHE328-LEU350
AMET356-ALA372
ATHR377-LEU399
ALEU408-TYR432

site_idSWS_FT_FI3
Number of Residues402
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:21677752
ChainResidueDetails
AALA38-SER98
AARG147-ASP154
ATRP195-SER199
ASER236-ALA239
AGLY281-VAL327
AGLY373-PHE376
ATYR433-ARG712

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21677752
ChainResidueDetails
AASP56
AASP154
AGLU319

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29058712
ChainResidueDetails
ATYR468
ATYR196
ATYR293
AARG375

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Interacts with target acceptor peptide in protein substrate => ECO:0000269|PubMed:21677752
ChainResidueDetails
AASP56
AGLU319
AILE572

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:21677752
ChainResidueDetails
AARG147

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Interacts with target acceptor peptide in protein substrate; important for extended sequon recognition => ECO:0000269|PubMed:21677752
ChainResidueDetails
AARG331

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (DATDGlc) asparagine => ECO:0000269|PubMed:21677752
ChainResidueDetails
AGLN535
APRO556

221051

PDB entries from 2024-06-12

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