Following evolutionary paths to high affinity and selectivity protein-protein interactions using Colicin7 and Immunity proteins. Determined by X-ray diffraction at 2.48 Å resolution. Released 15 Sept 2009.
Explore 3GJN in 3D Show helices and sheets RCSB PDB PDBe
3GJN contains 33 α-helices and 32 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 1007-1009 | 3 | |
| β-strand | 1011 | 1 | 1 |
| α-helix | 1012-1022 | 11 | |
| β-strand | 1025 | 1 | 2 |
| β-strand | 1028 | 1 | 2 |
| α-helix | 1030-1044 | 15 | |
| α-helix | 1051-1054 | 4 | |
| α-helix | 1056-1057 | 2 | |
| α-helix | 1064-1077 | 14 | |
| β-strand | 1084 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 454 | 1 | 3 |
| β-strand | 458 | 1 | 4 |
| α-helix | 464-467 | 4 | |
| β-strand | 474-475 | 2 | 5 |
| α-helix | 476 | 1 | |
| β-strand | 477 | 1 | 4 |
| α-helix | 478-484 | 7 | |
| α-helix | 492-503 | 12 | |
| α-helix | 507-510 | 4 | |
| α-helix | 515-522 | 8 | |
| α-helix | 525-527 | 3 | |
| β-strand | 528 | 1 | 6 |
| α-helix | 529-530 | 2 | |
| α-helix | 531-533 | 3 | |
| β-strand | 535 | 1 | 7 |
| β-strand | 538 | 1 | 7 |
| β-strand | 540 | 1 | 6 |
| β-strand | 542-545 | 4 | 5 |
| β-strand | 557 | 1 | 3 |
| α-helix | 558-560 | 3 | |
| β-strand | 561-564 | 4 | 5 |
| α-helix | 566-573 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 451 | 1 | 8 |
| β-strand | 454 | 1 | 9 |
| β-strand | 458 | 1 | 10 |
| α-helix | 464-469 | 6 | |
| β-strand | 474-475 | 2 | 11 |
| α-helix | 476 | 1 | |
| β-strand | 477 | 1 | 10 |
| α-helix | 478-484 | 7 | |
| β-strand | 489 | 1 | 8 |
| α-helix | 492-505 | 14 | |
| α-helix | 507-510 | 4 | |
| α-helix | 515-522 | 8 | |
| α-helix | 525-527 | 3 | |
| β-strand | 528 | 1 | 12 |
| α-helix | 529-530 | 2 | |
| α-helix | 531-533 | 3 | |
| β-strand | 535 | 1 | 13 |
| β-strand | 538 | 1 | 13 |
| β-strand | 540 | 1 | 12 |
| β-strand | 542-545 | 4 | 11 |
| β-strand | 557 | 1 | 9 |
| α-helix | 558-560 | 3 | |
| β-strand | 561-564 | 4 | 11 |
| α-helix | 566-573 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1007-1009 | 3 | |
| β-strand | 1011 | 1 | 14 |
| α-helix | 1012-1022 | 11 | |
| β-strand | 1025 | 1 | 15 |
| β-strand | 1028 | 1 | 15 |
| α-helix | 1030-1044 | 15 | |
| α-helix | 1051-1054 | 4 | |
| α-helix | 1064-1077 | 14 | |
| β-strand | 1084 | 1 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Colicin-E9 immunity protein | A, D | protein | 86 | Escherichia coli | P13479 (AlphaFold model) |
| Colicin-E7 | B, C | protein | 141 | Escherichia coli | Q47112 (AlphaFold model) |
>3GJN_1 Colicin-E9 immunity protein (chains A, D) MELKHSISDYTEAEFLQLVTTICDAEATSEEELDKLITHFEEMTEHPSGSDLIYWPKEGD DDSPSGIVNTVKQWRAANGKSGFKQG
>3GJN_2 Colicin-E7 (chains B, C) MHHHHHHSMGKRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDF RKKFWEEVSKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKRTSFELHAEKPISQNGGV YDMDNISVVTPKRHIDIHRGK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Following evolutionary paths to protein-protein interactions with high affinity and selectivity. Levin, K.B., Dym, O., Albeck, S. et al. Nat Struct Mol Biol (2009) 16:1049-1055. DOI 10.1038/nsmb.1670 · PubMed
Other PDB entries of the same protein (UniProt P13479 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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