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 |