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
| Chain | GOid | namespace | contents |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0015288 | molecular_function | porin activity |
| A | 0016020 | cellular_component | membrane |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0015288 | molecular_function | porin activity |
| B | 0016020 | cellular_component | membrane |
| C | 0009279 | cellular_component | cell outer membrane |
| C | 0015288 | molecular_function | porin activity |
| C | 0016020 | cellular_component | membrane |
| D | 0001618 | molecular_function | virus receptor activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0006974 | biological_process | DNA damage response |
| D | 0009279 | cellular_component | cell outer membrane |
| D | 0015288 | molecular_function | porin activity |
| D | 0016020 | cellular_component | membrane |
| D | 0034220 | biological_process | monoatomic ion transmembrane transport |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046718 | biological_process | symbiont entry into host cell |
| D | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046930 | cellular_component | pore complex |
| D | 0120010 | biological_process | intermembrane phospholipid transfer |
Functional Information from PROSITE/UniProt
| site_id | PS00576 |
| Number of Residues | 17 |
| Details | GRAM_NEG_PORIN General diffusion Gram-negative porins signature. VdvGatYyFnKnmSTYV |
| Chain | Residue | Details |
| D | VAL298-VAL314 |
| site_id | PS01068 |
| Number of Residues | 45 |
| Details | OMPA_1 OmpA-like domain. VlGyTDri.GSdaYNqgLSERRAqsVvdyLiskg.IpadkIsarGmG |
| Chain | Residue | Details |
| A | VAL236-GLY280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"11276254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9808047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 171 |
| Details | Transmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"11276254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9808047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 51 |
| Details | Transmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"9808047","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11276254","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 60 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"9808047","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11276254","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Part of salt bridge gating mechanism","evidences":[{"source":"PubMed","id":"17041590","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"O3-poly(beta-hydroxybutyryl)serine","evidences":[{"source":"PubMed","id":"17659252","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"16949612","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 133 |
| Details | Transmembrane: {"description":"Beta stranded"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 135 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"16949612","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 17 |
| Details | Region: {"description":"Loop L3; may constrict the pore"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2J1N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
