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3NB3

The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components

Functional Information from GO Data
ChainGOidnamespacecontents
A0009279cellular_componentcell outer membrane
A0015288molecular_functionporin activity
A0016020cellular_componentmembrane
B0009279cellular_componentcell outer membrane
B0015288molecular_functionporin activity
B0016020cellular_componentmembrane
C0009279cellular_componentcell outer membrane
C0015288molecular_functionporin activity
C0016020cellular_componentmembrane
D0001618molecular_functionvirus receptor activity
D0005515molecular_functionprotein binding
D0006811biological_processmonoatomic ion transport
D0006974biological_processDNA damage response
D0009279cellular_componentcell outer membrane
D0015288molecular_functionporin activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0042802molecular_functionidentical protein binding
D0046718biological_processsymbiont entry into host cell
D0046813biological_processreceptor-mediated virion attachment to host cell
D0046872molecular_functionmetal ion binding
D0046930cellular_componentpore complex
Functional Information from PROSITE/UniProt
site_idPS00576
Number of Residues17
DetailsGRAM_NEG_PORIN General diffusion Gram-negative porins signature. VdvGatYyFnKnmSTYV
ChainResidueDetails
DVAL298-VAL314

site_idPS01068
Number of Residues45
DetailsOMPA_1 OmpA-like domain. VlGyTDri.GSdaYNqgLSERRAqsVvdyLiskg.IpadkIsarGmG
ChainResidueDetails
AVAL236-GLY280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:16949612
ChainResidueDetails
DALA1-ASP12
CASN46-TYR48
CILE87-ASP90
CILE131-GLU134
DGLU43-GLY52
DLYS81-VAL85
DTHR134-GLY142
DASP187-GLY190
DASP228-ASN231
DGLN266-GLY270
DPHE306-ASN309
DPHE346

site_idSWS_FT_FI2
Number of Residues133
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
DLEU13-HIS21
DTYR221-TYR227
DILE232-THR239
DSER249-TYR265
DLEU271-LEU278
DVAL298-TYR305
DMET310-LYS317
DVAL338-GLN345
CILE135-TRP143
CMET161-PHE170
DGLN33-GLY42
DTYR53-ASN63
DSER71-LEU80
DGLY86-TYR94
DMET121-ASN133
DLEU143-GLN150
DVAL180-TYR186
DPHE191-SER198

site_idSWS_FT_FI3
Number of Residues135
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:16949612
ChainResidueDetails
DTYR22-ASP32
DSER64-ASN70
DGLY95-PHE120
DGLY151-GLY179
DSER199-THR220
DGLN240-GLY248
DGLN279-TYR297
DILE318-ILE337

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:2J1N
ChainResidueDetails
DASN319
DLEU321
DTHR334
BPRO121-ALA130
CLEU91-GLY99
CPRO121-ALA130

site_idSWS_FT_FI5
Number of Residues108
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:9808047, ECO:0000305|PubMed:11276254
ChainResidueDetails
AMET100-SER120
ATHR144-GLY160
BMET100-SER120
BTHR144-GLY160
CMET100-SER120
CTHR144-GLY160

site_idSWS_FT_FI6
Number of Residues462
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:11276254, ECO:0000305|PubMed:9808047
ChainResidueDetails
AGLY171-ALA325
BGLY171-ALA325
CGLY171-ALA325

site_idSWS_FT_FI7
Number of Residues6
DetailsSITE: Part of salt bridge gating mechanism => ECO:0000269|PubMed:17041590
ChainResidueDetails
AGLU52
AARG138
BGLU52
BARG138
CGLU52
CARG138

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: O3-poly(beta-hydroxybutyryl)serine => ECO:0000269|PubMed:17659252
ChainResidueDetails
ASER163
ASER167
BSER163
BSER167
CSER163
CSER167

222036

PDB entries from 2024-07-03

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