Chemical shift structure of COLICIN E9 DNASE domain with its cognate immunity protein IM9. Determined by solution NMR. Released 9 Dec 2008.
Explore 2K5X in 3D Show helices and sheets RCSB PDB PDBe
2K5X contains 14 α-helices and 15 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 | 12-23 | 12 | |
| α-helix | 30-44 | 15 | |
| α-helix | 50-54 | 5 | |
| α-helix | 56-57 | 2 | |
| β-strand | 58 | 1 | 1 |
| β-strand | 60 | 1 | 1 |
| α-helix | 64-78 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-10 | 2 | 2 |
| β-strand | 12 | 1 | 3 |
| β-strand | 16 | 1 | 4 |
| α-helix | 22-25 | 4 | |
| β-strand | 32-33 | 2 | 5 |
| α-helix | 34 | 1 | |
| β-strand | 35 | 1 | 4 |
| α-helix | 36-40 | 5 | |
| β-strand | 46-47 | 2 | 2 |
| α-helix | 50-63 | 14 | |
| α-helix | 73-80 | 8 | |
| β-strand | 86 | 1 | 6 |
| β-strand | 93 | 1 | 7 |
| β-strand | 96 | 1 | 7 |
| β-strand | 98 | 1 | 6 |
| β-strand | 100-103 | 4 | 5 |
| α-helix | 107-109 | 3 | |
| β-strand | 115 | 1 | 3 |
| α-helix | 116-118 | 3 | |
| β-strand | 119-122 | 4 | 5 |
| α-helix | 124-130 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Colicin-E9 immunity protein | A | protein | 86 | Escherichia coli | P13479 (AlphaFold model) |
| Colicin-E9 | B | protein | 134 | Escherichia coli | P09883 (AlphaFold model) |
>2K5X_1 Colicin-E9 immunity protein (chains A) MELKHSISDYTEAEFLQLVTTICNADTSSEEELVKLVTHFEEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGKSGFKQG
>2K5X_2 Colicin-E9 (chains B) MESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEE VSKDPELSKNLNPSNKSSVSKGYSPFTPKNQQVGGRKVYELHHDKPISQGGEVYDMDNIR VTTPKRHIDIHRGK
Structure Determination of Protein-Protein Complexes Using NMR Chemical Shifts: Case of an Endonuclease Colicin-Immunity Protein Complex. Montalvao, R.W., Cavalli, A., Salvatella, X. et al. J Am Chem Soc (2008) 130:15990-15996. 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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