osmoporin OmpC. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Sept 2006.
Explore 2J1N in 3D Show helices and sheets RCSB PDB PDBe
2J1N contains 22 α-helices and 77 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| β-strand | 9-23 | 15 | 1 |
| β-strand | 31-32 | 2 | 1 |
| β-strand | 35-45 | 11 | 1 |
| β-strand | 50-61 | 12 | 1 |
| β-strand | 71-82 | 12 | 1 |
| β-strand | 86-94 | 9 | 1 |
| α-helix | 98-101 | 4 | |
| α-helix | 102-104 | 3 | |
| β-strand | 124-134 | 11 | 1 |
| α-helix | 135-138 | 4 | |
| β-strand | 143-150 | 8 | 1 |
| β-strand | 153 | 1 | 2 |
| β-strand | 155 | 1 | 3 |
| α-helix | 156 | 1 | |
| β-strand | 165 | 1 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 176 | 1 | 2 |
| β-strand | 179-188 | 10 | 1 |
| β-strand | 191-201 | 11 | 1 |
| α-helix | 202-203 | 2 | |
| β-strand | 212 | 1 | 4 |
| β-strand | 217-229 | 13 | 1 |
| β-strand | 232-242 | 11 | 1 |
| β-strand | 246 | 1 | 5 |
| β-strand | 251 | 1 | 4 |
| β-strand | 252 | 1 | 5 |
| β-strand | 255-265 | 11 | 1 |
| β-strand | 271-283 | 13 | 1 |
| β-strand | 292-305 | 14 | 1 |
| β-strand | 310-319 | 10 | 1 |
| α-helix | 325-330 | 6 | |
| β-strand | 337-345 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 9-23 | 15 | 6 |
| β-strand | 31-32 | 2 | 6 |
| β-strand | 35-45 | 11 | 6 |
| β-strand | 50-61 | 12 | 6 |
| β-strand | 71-82 | 12 | 6 |
| β-strand | 86-94 | 9 | 6 |
| α-helix | 98-101 | 4 | |
| α-helix | 102-104 | 3 | |
| β-strand | 124-133 | 10 | 6 |
| β-strand | 143-150 | 8 | 6 |
| β-strand | 153 | 1 | 7 |
| β-strand | 155 | 1 | 8 |
| α-helix | 156 | 1 | |
| β-strand | 165 | 1 | 8 |
| α-helix | 172-174 | 3 | |
| β-strand | 176 | 1 | 7 |
| β-strand | 179-188 | 10 | 6 |
| β-strand | 191-201 | 11 | 6 |
| α-helix | 202-203 | 2 | |
| β-strand | 212 | 1 | 9 |
| β-strand | 217-229 | 13 | 6 |
| β-strand | 232-242 | 11 | 6 |
| β-strand | 246 | 1 | 10 |
| β-strand | 251 | 1 | 9 |
| β-strand | 252 | 1 | 10 |
| β-strand | 255-265 | 11 | 6 |
| β-strand | 271-283 | 13 | 6 |
| β-strand | 292-307 | 16 | 6 |
| β-strand | 310-319 | 10 | 6 |
| α-helix | 325-330 | 6 | |
| β-strand | 337-345 | 9 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 11 |
| β-strand | 9-23 | 15 | 11 |
| β-strand | 31-32 | 2 | 11 |
| β-strand | 35-45 | 11 | 11 |
| β-strand | 50-61 | 12 | 11 |
| β-strand | 71-82 | 12 | 11 |
| β-strand | 86-94 | 9 | 11 |
| α-helix | 98-101 | 4 | |
| α-helix | 102-104 | 3 | |
| β-strand | 124-133 | 10 | 11 |
| α-helix | 135-138 | 4 | |
| β-strand | 143-150 | 8 | 11 |
| β-strand | 153 | 1 | 12 |
| β-strand | 155 | 1 | 13 |
| α-helix | 156 | 1 | |
| β-strand | 165 | 1 | 13 |
| α-helix | 172-174 | 3 | |
| β-strand | 176 | 1 | 12 |
| β-strand | 179-188 | 10 | 11 |
| β-strand | 191-201 | 11 | 11 |
| α-helix | 202-203 | 2 | |
| α-helix | 204-206 | 3 | |
| β-strand | 212 | 1 | 14 |
| β-strand | 217-229 | 13 | 11 |
| β-strand | 232-242 | 11 | 11 |
| β-strand | 246-247 | 2 | 14 |
| β-strand | 251-252 | 2 | 14 |
| β-strand | 255-265 | 11 | 11 |
| β-strand | 271-283 | 13 | 11 |
| β-strand | 292-307 | 16 | 11 |
| β-strand | 310-319 | 10 | 11 |
| α-helix | 321-323 | 3 | |
| α-helix | 325-330 | 6 | |
| β-strand | 337-345 | 9 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Outer membrane protein C | A, B, C | protein | 346 | ESCHERICHIA COLI | P06996 (AlphaFold model) |
>2J1N_1 OUTER MEMBRANE PROTEIN C (chains A, B, C) AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQI QGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNF MQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGV GGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQ TYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDV GATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF
Water and common crystallization additives (CL) are not listed.
Crystal Structure of Osmoporin Ompc from E. Coli at 2.0 A. Basle, A., Rummel, G., Storici, P. et al. J Mol Biol (2006) 362:933. DOI 10.1016/J.JMB.2006.08.002 · PubMed
Other PDB entries of the same protein (UniProt P06996 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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