Crystal structure of the mutant H573A of the nuclease domain of COLE7 in complex with IM7. Determined by X-ray diffraction at 1.91 Å resolution. Released 3 Apr 2007.
Explore 2JB0 in 3D Show helices and sheets RCSB PDB PDBe
2JB0 contains 15 α-helices and 13 β-strands across 2 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 | 7-9 | 3 | |
| α-helix | 12-26 | 15 | |
| α-helix | 32-45 | 14 | |
| α-helix | 52-55 | 4 | |
| α-helix | 65-78 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 451-452 | 2 | 1 |
| β-strand | 454 | 1 | 2 |
| β-strand | 458 | 1 | 3 |
| α-helix | 464-467 | 4 | |
| β-strand | 474-475 | 2 | 4 |
| α-helix | 476 | 1 | |
| β-strand | 477 | 1 | 3 |
| α-helix | 478-484 | 7 | |
| β-strand | 488-489 | 2 | 1 |
| α-helix | 492-505 | 14 | |
| α-helix | 507-510 | 4 | |
| α-helix | 515-522 | 8 | |
| α-helix | 525-527 | 3 | |
| β-strand | 528 | 1 | 5 |
| α-helix | 531-533 | 3 | |
| β-strand | 535 | 1 | 6 |
| β-strand | 538 | 1 | 6 |
| β-strand | 540 | 1 | 5 |
| β-strand | 542-545 | 4 | 4 |
| β-strand | 557 | 1 | 2 |
| α-helix | 558-560 | 3 | |
| β-strand | 561-564 | 4 | 4 |
| α-helix | 566-571 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Colicin E7 immunity protein | A | protein | 87 | ESCHERICHIA COLI | Q03708 (AlphaFold model) |
| Colicin E7 | B | protein | 131 | ESCHERICHIA COLI | Q47112 (AlphaFold model) |
>2JB0_1 COLICIN E7 IMMUNITY PROTEIN (chains A) MELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDN RDDSPEGIVKEIKEWRAANGKPGFKQG
>2JB0_2 COLICIN E7 (chains B) KRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEVSK DPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKRTSFELHHEKPISQNGGVYDMDNISVVT PKRHIDIARGK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
The Conserved Asparagine in the Hnh Motif Serves an Important Structural Role in Metal Finger Endonucleases. Huang, H., Yuan, H.S. J Mol Biol (2007) 368:812. DOI 10.1016/J.JMB.2007.02.044 · PubMed
Other PDB entries of the same protein (UniProt Q03708 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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