4LSI
Ion selectivity of OmpF porin soaked in 0.3M KBr
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 | 0001530 | molecular_function | lipopolysaccharide binding |
| B | 0005216 | molecular_function | monoatomic ion channel activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0015031 | biological_process | protein transport |
| B | 0015288 | molecular_function | porin activity |
| B | 0016020 | cellular_component | membrane |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0034702 | cellular_component | monoatomic ion channel complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042912 | molecular_function | colicin transmembrane transporter activity |
| B | 0043213 | biological_process | bacteriocin transport |
| B | 0046930 | cellular_component | pore complex |
| B | 0070207 | biological_process | protein homotrimerization |
| B | 0097718 | molecular_function | disordered domain specific binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 401 |
| Chain | Residue |
| A | ASP121 |
| A | HOH652 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 402 |
| Chain | Residue |
| A | ASP113 |
| A | MET114 |
| A | ARG270 |
| A | HOH666 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE C8E A 403 |
| Chain | Residue |
| A | LEU227 |
| A | ALA228 |
| A | VAL260 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ARG82 |
| A | ASP113 |
| A | ARG132 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | VAL11 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 406 |
| Chain | Residue |
| A | GLU201 |
| A | GLN203 |
| A | GLY206 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 407 |
| Chain | Residue |
| A | ASN316 |
| A | ILE318 |
| A | SER328 |
| A | HOH557 |
| A | HOH595 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 408 |
| Chain | Residue |
| A | SER125 |
| A | ARG167 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 409 |
| Chain | Residue |
| A | HOH514 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BR A 410 |
| Chain | Residue |
| A | TYR102 |
| A | GLY103 |
| A | VAL104 |
| A | TYR106 |
| A | PHE129 |
| A | VAL130 |
| A | GLY131 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BR A 411 |
| Chain | Residue |
| A | MET114 |
| A | LEU115 |
| A | PRO116 |
| A | GLN262 |
| A | SER272 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG A 412 |
| Chain | Residue |
| A | GLN66 |
| A | GLY67 |
| A | ASN68 |
| A | ASN69 |
| A | SER70 |
| A | ALA75 |
| A | ASN79 |
| C | LYS80 |
| C | THR81 |
| C | ARG100 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG B 401 |
| Chain | Residue |
| A | LYS80 |
| A | THR81 |
| A | ARG100 |
| B | GLN66 |
| B | ASN69 |
| B | SER70 |
| B | GLU71 |
| B | ALA75 |
| B | ASN79 |
| B | HOH503 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 402 |
| Chain | Residue |
| B | HOH639 |
| B | HOH646 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 403 |
| Chain | Residue |
| B | ARG140 |
| B | ASN141 |
| B | SER142 |
| B | PHE153 |
| B | SER177 |
| B | SER179 |
| B | HOH656 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE C8E B 404 |
| Chain | Residue |
| B | PHE267 |
| B | TYR301 |
| C | TYR313 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE C8E B 405 |
| Chain | Residue |
| B | LEU259 |
| B | ILE273 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 406 |
| Chain | Residue |
| B | ARG82 |
| B | ASP113 |
| B | ARG132 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 407 |
| Chain | Residue |
| B | GLU201 |
| B | GLN203 |
| B | GLY206 |
| B | HOH601 |
| B | HOH673 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 408 |
| Chain | Residue |
| B | ASN316 |
| B | ILE318 |
| B | SER328 |
| B | HOH600 |
| C | HOH663 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 410 |
| Chain | Residue |
| B | SER125 |
| B | ARG167 |
| site_id | CC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 411 |
| Chain | Residue |
| B | ILE51 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE C8E C 401 |
| Chain | Residue |
| C | TYR98 |
| C | GLY159 |
| C | GLY173 |
| C | HOH586 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 402 |
| Chain | Residue |
| C | ASN207 |
| C | ASN236 |
| C | ASN252 |
| C | HOH588 |
| C | HOH593 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 403 |
| Chain | Residue |
| B | HOH532 |
| C | ASN69 |
| C | ASP74 |
| C | HOH636 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 404 |
| Chain | Residue |
| C | GLU201 |
| C | GLN203 |
| C | GLY206 |
| C | HOH606 |
| C | HOH676 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 405 |
| Chain | Residue |
| C | ASN316 |
| C | ILE318 |
| C | SER328 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG C 406 |
| Chain | Residue |
| C | ASP126 |
| C | ASP127 |
| C | PHE128 |
| C | GLY134 |
| C | ARG163 |
| C | ARG167 |
| C | ARG168 |
| C | SER169 |
| C | ASN170 |
| C | GLN200 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG C 407 |
| Chain | Residue |
| B | LYS80 |
| B | THR81 |
| C | GLN66 |
| C | ASN69 |
| C | SER70 |
| C | GLU71 |
| C | ALA75 |
| C | ASN79 |
| C | HOH504 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 409 |
| Chain | Residue |
| C | ASP113 |
| C | ARG132 |
| C | HOH640 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR C 410 |
| Chain | Residue |
| C | LYS16 |
| C | HOH506 |
| C | HOH600 |
| site_id | DC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR C 411 |
| Chain | Residue |
| C | SER125 |
| C | ARG167 |
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 |
| A | PHE295-VAL311 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 510 |
| Details | TRANSMEM: Beta stranded |
| Chain | Residue | Details |
| A | ALA1-LYS6 | |
| A | GLY184-ASP195 | |
| A | ALA211-ALA222 | |
| A | ASN224-ARG235 | |
| A | LYS253-PHE265 | |
| A | GLY268-LYS281 | |
| A | VAL292-PHE303 | |
| A | ASN306-ILE315 | |
| A | THR331-PHE340 | |
| B | ALA1-LYS6 | |
| B | GLY8-PHE23 | |
| A | GLY8-PHE23 | |
| B | THR39-ILE51 | |
| B | ASP54-GLN66 | |
| B | LEU83-ALA91 | |
| B | GLY94-ARG100 | |
| B | GLY135-ASN141 | |
| B | GLY150-GLY159 | |
| B | ASP172-TYR182 | |
| B | GLY184-ASP195 | |
| B | ALA211-ALA222 | |
| B | ASN224-ARG235 | |
| A | THR39-ILE51 | |
| B | LYS253-PHE265 | |
| B | GLY268-LYS281 | |
| B | VAL292-PHE303 | |
| B | ASN306-ILE315 | |
| B | THR331-PHE340 | |
| C | ALA1-LYS6 | |
| C | GLY8-PHE23 | |
| C | THR39-ILE51 | |
| C | ASP54-GLN66 | |
| C | LEU83-ALA91 | |
| A | ASP54-GLN66 | |
| C | GLY94-ARG100 | |
| C | GLY135-ASN141 | |
| C | GLY150-GLY159 | |
| C | ASP172-TYR182 | |
| C | GLY184-ASP195 | |
| C | ALA211-ALA222 | |
| C | ASN224-ARG235 | |
| C | LYS253-PHE265 | |
| C | GLY268-LYS281 | |
| C | VAL292-PHE303 | |
| A | LEU83-ALA91 | |
| C | ASN306-ILE315 | |
| C | THR331-PHE340 | |
| A | GLY94-ARG100 | |
| A | GLY135-ASN141 | |
| A | GLY150-GLY159 | |
| A | ASP172-TYR182 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASN52-SER53 | |
| B | ASP92-VAL93 | |
| B | SER142-ASP149 | |
| B | GLU183 | |
| B | ASN223 | |
| B | ASP266-PHE267 | |
| B | ASN304-LYS305 | |
| C | ASP7 | |
| C | ASN52-SER53 | |
| C | ASP92-VAL93 | |
| A | ASN52-SER53 | |
| C | SER142-ASP149 | |
| C | GLU183 | |
| C | ASN223 | |
| C | ASP266-PHE267 | |
| C | ASN304-LYS305 | |
| A | ASP92-VAL93 | |
| A | SER142-ASP149 | |
| A | GLU183 | |
| A | ASN223 | |
| A | ASP266-PHE267 | |
| A | ASN304-LYS305 | |
| B | ASP7 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 378 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| A | SER24-MET38 | |
| B | GLY67-ARG82 | |
| B | ASN101-GLY134 | |
| B | LYS160-GLY171 | |
| B | ARG196-LYS210 | |
| B | ASN236-ASN252 | |
| B | ASP282-LEU291 | |
| B | ASN316-ASP330 | |
| C | SER24-MET38 | |
| C | GLY67-ARG82 | |
| C | ASN101-GLY134 | |
| A | GLY67-ARG82 | |
| C | LYS160-GLY171 | |
| C | ARG196-LYS210 | |
| C | ASN236-ASN252 | |
| C | ASP282-LEU291 | |
| C | ASN316-ASP330 | |
| A | ASN101-GLY134 | |
| A | LYS160-GLY171 | |
| A | ARG196-LYS210 | |
| A | ASN236-ASN252 | |
| A | ASP282-LEU291 | |
| A | ASN316-ASP330 | |
| B | SER24-MET38 |
