5NUO
Structural basis for maintenance of bacterial outer membrane lipid asymmetry
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001530 | molecular_function | lipopolysaccharide binding |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0015031 | biological_process | protein transport |
| A | 0015288 | molecular_function | porin activity |
| A | 0016020 | cellular_component | membrane |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034702 | cellular_component | monoatomic ion channel complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042912 | molecular_function | colicin transmembrane transporter activity |
| A | 0043213 | biological_process | bacteriocin transport |
| A | 0046930 | cellular_component | pore complex |
| A | 0070207 | biological_process | protein homotrimerization |
| A | 0097718 | molecular_function | disordered domain specific binding |
| B | 0016020 | cellular_component | membrane |
| B | 0120010 | biological_process | intermembrane phospholipid transfer |
| C | 0001530 | molecular_function | lipopolysaccharide binding |
| C | 0005216 | molecular_function | monoatomic ion channel activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0008289 | molecular_function | lipid binding |
| C | 0009279 | cellular_component | cell outer membrane |
| C | 0015031 | biological_process | protein transport |
| C | 0015288 | molecular_function | porin activity |
| C | 0016020 | cellular_component | membrane |
| C | 0034220 | biological_process | monoatomic ion transmembrane transport |
| C | 0034702 | cellular_component | monoatomic ion channel complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042912 | molecular_function | colicin transmembrane transporter activity |
| C | 0043213 | biological_process | bacteriocin transport |
| C | 0046930 | cellular_component | pore complex |
| C | 0070207 | biological_process | protein homotrimerization |
| C | 0097718 | molecular_function | disordered domain specific binding |
| D | 0016020 | cellular_component | membrane |
| D | 0120010 | biological_process | intermembrane phospholipid transfer |
| E | 0001530 | molecular_function | lipopolysaccharide binding |
| E | 0005216 | molecular_function | monoatomic ion channel activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0006811 | biological_process | monoatomic ion transport |
| E | 0008289 | molecular_function | lipid binding |
| E | 0009279 | cellular_component | cell outer membrane |
| E | 0015031 | biological_process | protein transport |
| E | 0015288 | molecular_function | porin activity |
| E | 0016020 | cellular_component | membrane |
| E | 0034220 | biological_process | monoatomic ion transmembrane transport |
| E | 0034702 | cellular_component | monoatomic ion channel complex |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0042912 | molecular_function | colicin transmembrane transporter activity |
| E | 0043213 | biological_process | bacteriocin transport |
| E | 0046930 | cellular_component | pore complex |
| E | 0070207 | biological_process | protein homotrimerization |
| E | 0097718 | molecular_function | disordered domain specific binding |
| F | 0016020 | cellular_component | membrane |
| F | 0120010 | biological_process | intermembrane phospholipid transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 401 |
| Chain | Residue |
| C | THR165 |
| C | ARG167 |
| C | ARG168 |
| E | GLY72 |
| E | ALA73 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| C | ARG42 |
| C | ARG82 |
| C | ARG132 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue C8E C 403 |
| Chain | Residue |
| C | PHE265 |
| C | C8E404 |
| C | C8E405 |
| D | TYR79 |
| C | TYR263 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue C8E C 404 |
| Chain | Residue |
| C | ILE225 |
| C | TYR263 |
| C | C8E403 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue C8E C 405 |
| Chain | Residue |
| C | VAL297 |
| C | GLY298 |
| C | C8E403 |
| D | PHE85 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue C8E C 406 |
| Chain | Residue |
| C | VAL93 |
| C | PHE145 |
| F | PRO51 |
| F | ALA52 |
| F | ASN54 |
| F | ASN58 |
| F | ASP101 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue C8E D 301 |
| Chain | Residue |
| A | C8E403 |
| C | PHE23 |
| D | PHE88 |
| D | ILE93 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue C8E D 302 |
| Chain | Residue |
| A | VAL93 |
| A | PHE145 |
| D | PRO51 |
| D | ASN54 |
| D | ASN58 |
| D | LEU99 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue C8E D 303 |
| Chain | Residue |
| B | PHE137 |
| D | VAL127 |
| D | GLY128 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue C8E D 304 |
| Chain | Residue |
| D | TYR138 |
| D | PHE141 |
| D | TRP170 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue C8E D 305 |
| Chain | Residue |
| D | ASN28 |
| D | LEU37 |
| D | PHE137 |
| D | TRP170 |
| D | GLY174 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | ARG42 |
| A | ARG82 |
| A | ARG132 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | THR165 |
| A | ARG168 |
| C | GLY72 |
| C | ALA73 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue C8E A 403 |
| Chain | Residue |
| A | TYR157 |
| D | ILE93 |
| D | MET96 |
| D | C8E301 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue C8E A 404 |
| Chain | Residue |
| A | GLY176 |
| A | TYR191 |
| A | C8E406 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue C8E A 405 |
| Chain | Residue |
| A | TYR263 |
| B | C8E301 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue C8E A 406 |
| Chain | Residue |
| A | TYR191 |
| A | ARG235 |
| A | C8E404 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue C8E B 301 |
| Chain | Residue |
| A | TYR263 |
| A | PHE265 |
| A | C8E405 |
| B | PRO78 |
| B | TYR79 |
| B | GLN109 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 E 401 |
| Chain | Residue |
| A | GLY72 |
| A | ALA73 |
| E | THR165 |
| E | ARG167 |
| E | ARG168 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue C8E E 403 |
| Chain | Residue |
| E | VAL297 |
| E | GLY298 |
| F | PHE85 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue C8E E 404 |
| Chain | Residue |
| C | TYR98 |
| E | HIS21 |
| E | VAL334 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue C8E E 405 |
| Chain | Residue |
| E | ILE225 |
| E | TYR263 |
| F | C8E302 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue C8E E 406 |
| Chain | Residue |
| E | GLU48 |
| E | TYR58 |
| E | LYS89 |
| E | SER142 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue C8E F 301 |
| Chain | Residue |
| F | ILE93 |
| F | MET96 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue C8E F 302 |
| Chain | Residue |
| E | PHE265 |
| E | C8E405 |
| F | TYR79 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide SO4 E 402 and ARG E 82 |
| Chain | Residue |
| E | LEU83 |
| E | ARG100 |
| E | ARG132 |
| E | ARG42 |
| E | GLU62 |
| E | THR81 |
Functional Information from PROSITE/UniProt
| site_id | PS00576 |
| Number of Residues | 17 |
| Details | GRAM_NEG_PORIN General diffusion Gram-negative porins signature. FevGatYyFnKnmSTYV |
| Chain | Residue | Details |
| C | PHE295-VAL311 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 510 |
| Details | TRANSMEM: Beta stranded |
| Chain | Residue | Details |
| C | ALA1-LYS6 | |
| C | GLY184-ASP195 | |
| C | ALA211-ALA222 | |
| C | ASN224-ARG235 | |
| C | LYS253-PHE265 | |
| C | GLY268-LYS281 | |
| C | VAL292-PHE303 | |
| C | ASN306-ILE315 | |
| C | THR331-PHE340 | |
| A | ALA1-LYS6 | |
| A | GLY8-PHE23 | |
| C | GLY8-PHE23 | |
| A | THR39-ILE51 | |
| A | ASP54-GLN66 | |
| A | LEU83-ALA91 | |
| A | GLY94-ARG100 | |
| A | GLY135-ASN141 | |
| A | GLY150-GLY159 | |
| A | ASP172-TYR182 | |
| A | GLY184-ASP195 | |
| A | ALA211-ALA222 | |
| A | ASN224-ARG235 | |
| C | THR39-ILE51 | |
| A | LYS253-PHE265 | |
| A | GLY268-LYS281 | |
| A | VAL292-PHE303 | |
| A | ASN306-ILE315 | |
| A | THR331-PHE340 | |
| E | ALA1-LYS6 | |
| E | GLY8-PHE23 | |
| E | THR39-ILE51 | |
| E | ASP54-GLN66 | |
| E | LEU83-ALA91 | |
| C | ASP54-GLN66 | |
| E | GLY94-ARG100 | |
| E | GLY135-ASN141 | |
| E | GLY150-GLY159 | |
| E | ASP172-TYR182 | |
| E | GLY184-ASP195 | |
| E | ALA211-ALA222 | |
| E | ASN224-ARG235 | |
| E | LYS253-PHE265 | |
| E | GLY268-LYS281 | |
| E | VAL292-PHE303 | |
| C | LEU83-ALA91 | |
| E | ASN306-ILE315 | |
| E | THR331-PHE340 | |
| C | GLY94-ARG100 | |
| C | GLY135-ASN141 | |
| C | GLY150-GLY159 | |
| C | ASP172-TYR182 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| C | ASP7 | |
| A | ASN52-SER53 | |
| A | ASP92-VAL93 | |
| A | SER142-ASP149 | |
| A | GLU183 | |
| A | ASN223 | |
| A | ASP266-PHE267 | |
| A | ASN304-LYS305 | |
| E | ASP7 | |
| E | ASN52-SER53 | |
| E | ASP92-VAL93 | |
| C | ASN52-SER53 | |
| E | SER142-ASP149 | |
| E | GLU183 | |
| E | ASN223 | |
| E | ASP266-PHE267 | |
| E | ASN304-LYS305 | |
| C | ASP92-VAL93 | |
| C | SER142-ASP149 | |
| C | GLU183 | |
| C | ASN223 | |
| C | ASP266-PHE267 | |
| C | ASN304-LYS305 | |
| A | ASP7 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 378 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| C | SER24-MET38 | |
| A | GLY67-ARG82 | |
| A | ASN101-GLY134 | |
| A | LYS160-GLY171 | |
| A | ARG196-LYS210 | |
| A | ASN236-ASN252 | |
| A | ASP282-LEU291 | |
| A | ASN316-ASP330 | |
| E | SER24-MET38 | |
| E | GLY67-ARG82 | |
| E | ASN101-GLY134 | |
| C | GLY67-ARG82 | |
| E | LYS160-GLY171 | |
| E | ARG196-LYS210 | |
| E | ASN236-ASN252 | |
| E | ASP282-LEU291 | |
| E | ASN316-ASP330 | |
| C | ASN101-GLY134 | |
| C | LYS160-GLY171 | |
| C | ARG196-LYS210 | |
| C | ASN236-ASN252 | |
| C | ASP282-LEU291 | |
| C | ASN316-ASP330 | |
| A | SER24-MET38 |
