2J1N
osmoporin OmpC
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001618 | molecular_function | virus receptor activity |
A | 0005515 | molecular_function | protein binding |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006974 | biological_process | DNA damage response |
A | 0009279 | cellular_component | cell outer membrane |
A | 0015288 | molecular_function | porin activity |
A | 0016020 | cellular_component | membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0042802 | molecular_function | identical protein binding |
A | 0046718 | biological_process | symbiont entry into host cell |
A | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
A | 0046872 | molecular_function | metal ion binding |
A | 0046930 | cellular_component | pore complex |
A | 0120010 | biological_process | intermembrane phospholipid transfer |
B | 0001618 | molecular_function | virus receptor activity |
B | 0005515 | molecular_function | protein binding |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006974 | biological_process | DNA damage response |
B | 0009279 | cellular_component | cell outer membrane |
B | 0015288 | molecular_function | porin activity |
B | 0016020 | cellular_component | membrane |
B | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0042802 | molecular_function | identical protein binding |
B | 0046718 | biological_process | symbiont entry into host cell |
B | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
B | 0046872 | molecular_function | metal ion binding |
B | 0046930 | cellular_component | pore complex |
B | 0120010 | biological_process | intermembrane phospholipid transfer |
C | 0001618 | molecular_function | virus receptor activity |
C | 0005515 | molecular_function | protein binding |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006974 | biological_process | DNA damage response |
C | 0009279 | cellular_component | cell outer membrane |
C | 0015288 | molecular_function | porin activity |
C | 0016020 | cellular_component | membrane |
C | 0034220 | biological_process | monoatomic ion transmembrane transport |
C | 0042802 | molecular_function | identical protein binding |
C | 0046718 | biological_process | symbiont entry into host cell |
C | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
C | 0046872 | molecular_function | metal ion binding |
C | 0046930 | cellular_component | pore complex |
C | 0120010 | biological_process | intermembrane phospholipid transfer |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A1347 |
Chain | Residue |
A | ASN319 |
A | LEU321 |
A | THR334 |
A | HOH2140 |
A | HOH2148 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B1347 |
Chain | Residue |
B | HOH2194 |
B | ASN319 |
B | LEU321 |
B | THR334 |
B | HOH2191 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B1348 |
Chain | Residue |
B | THR47 |
B | ASP48 |
C | THR47 |
C | ASP48 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B1349 |
Chain | Residue |
A | ASN69 |
B | ASN69 |
C | ASN69 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C1347 |
Chain | Residue |
C | ASN319 |
C | LEU321 |
C | THR334 |
C | HOH2189 |
C | HOH2191 |
C | HOH2202 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE D12 C1348 |
Chain | Residue |
B | VAL338 |
C | TYR277 |
C | GLN279 |
C | D121350 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE D12 C1349 |
Chain | Residue |
A | TYR131 |
C | GLY194 |
C | GLY223 |
C | GLY224 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE D12 C1350 |
Chain | Residue |
B | LEU340 |
C | PHE259 |
C | D121348 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE D12 C1351 |
Chain | Residue |
A | TYR149 |
C | ILE197 |
C | THR222 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE D12 C1352 |
Chain | Residue |
C | LYS226 |
C | TYR227 |
C | VAL262 |
C | ALA276 |
C | TYR277 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D12 C1353 |
Chain | Residue |
C | TYR94 |
C | HOH2027 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE D12 C1354 |
Chain | Residue |
C | PHE23 |
C | ASN336 |
C | ILE337 |
C | VAL338 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 C1357 |
Chain | Residue |
A | ARG132 |
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 |
A | VAL298-VAL314 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 138 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:16949612 |
Chain | Residue | Details |
A | ALA1-ASP12 | |
B | ALA1-ASP12 | |
B | GLU43-GLY52 | |
B | LYS81-VAL85 | |
B | THR134-GLY142 | |
B | ASP187-GLY190 | |
B | ASP228-ASN231 | |
B | GLN266-GLY270 | |
B | PHE306-ASN309 | |
B | PHE346 | |
C | ALA1-ASP12 | |
A | GLU43-GLY52 | |
C | GLU43-GLY52 | |
C | LYS81-VAL85 | |
C | THR134-GLY142 | |
C | ASP187-GLY190 | |
C | ASP228-ASN231 | |
C | GLN266-GLY270 | |
C | PHE306-ASN309 | |
C | PHE346 | |
A | LYS81-VAL85 | |
A | THR134-GLY142 | |
A | ASP187-GLY190 | |
A | ASP228-ASN231 | |
A | GLN266-GLY270 | |
A | PHE306-ASN309 | |
A | PHE346 |
site_id | SWS_FT_FI2 |
Number of Residues | 399 |
Details | TRANSMEM: Beta stranded |
Chain | Residue | Details |
A | LEU13-HIS21 | |
A | TYR221-TYR227 | |
A | ILE232-THR239 | |
A | SER249-TYR265 | |
A | LEU271-LEU278 | |
A | VAL298-TYR305 | |
A | MET310-LYS317 | |
A | VAL338-GLN345 | |
B | LEU13-HIS21 | |
B | GLN33-GLY42 | |
B | TYR53-ASN63 | |
A | GLN33-GLY42 | |
B | SER71-LEU80 | |
B | GLY86-TYR94 | |
B | MET121-ASN133 | |
B | LEU143-GLN150 | |
B | VAL180-TYR186 | |
B | PHE191-SER198 | |
B | TYR221-TYR227 | |
B | ILE232-THR239 | |
B | SER249-TYR265 | |
B | LEU271-LEU278 | |
A | TYR53-ASN63 | |
B | VAL298-TYR305 | |
B | MET310-LYS317 | |
B | VAL338-GLN345 | |
C | LEU13-HIS21 | |
C | GLN33-GLY42 | |
C | TYR53-ASN63 | |
C | SER71-LEU80 | |
C | GLY86-TYR94 | |
C | MET121-ASN133 | |
C | LEU143-GLN150 | |
A | SER71-LEU80 | |
C | VAL180-TYR186 | |
C | PHE191-SER198 | |
C | TYR221-TYR227 | |
C | ILE232-THR239 | |
C | SER249-TYR265 | |
C | LEU271-LEU278 | |
C | VAL298-TYR305 | |
C | MET310-LYS317 | |
C | VAL338-GLN345 | |
A | GLY86-TYR94 | |
A | MET121-ASN133 | |
A | LEU143-GLN150 | |
A | VAL180-TYR186 | |
A | PHE191-SER198 |
site_id | SWS_FT_FI3 |
Number of Residues | 405 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:16949612 |
Chain | Residue | Details |
A | TYR22-ASP32 | |
B | SER64-ASN70 | |
B | GLY95-PHE120 | |
B | GLY151-GLY179 | |
B | SER199-THR220 | |
B | GLN240-GLY248 | |
B | GLN279-TYR297 | |
B | ILE318-ILE337 | |
C | TYR22-ASP32 | |
C | SER64-ASN70 | |
C | GLY95-PHE120 | |
A | SER64-ASN70 | |
C | GLY151-GLY179 | |
C | SER199-THR220 | |
C | GLN240-GLY248 | |
C | GLN279-TYR297 | |
C | ILE318-ILE337 | |
A | GLY95-PHE120 | |
A | GLY151-GLY179 | |
A | SER199-THR220 | |
A | GLN240-GLY248 | |
A | GLN279-TYR297 | |
A | ILE318-ILE337 | |
B | TYR22-ASP32 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0007744|PDB:2J1N |
Chain | Residue | Details |
A | ASN319 | |
A | LEU321 | |
A | THR334 | |
B | ASN319 | |
B | LEU321 | |
B | THR334 | |
C | ASN319 | |
C | LEU321 | |
C | THR334 |