Crystal Structure of the Colicin E9, mutant His103Ala, in complex with Mg+2 and dsDNA (resolution 2.9A). Determined by X-ray diffraction at 2.9 Å resolution. Released 23 Jun 2004.
Explore 1V14 in 3D Show helices and sheets RCSB PDB PDBe
1V14 contains 40 α-helices and 50 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 |
|---|---|---|---|
| β-strand | 9-10 | 2 | 1 |
| β-strand | 12 | 1 | 2 |
| β-strand | 16 | 1 | 3 |
| β-strand | 32 | 1 | 4 |
| β-strand | 35 | 1 | 3 |
| α-helix | 36-42 | 7 | |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-63 | 14 | |
| α-helix | 65-68 | 4 | |
| α-helix | 75-80 | 6 | |
| α-helix | 84-85 | 2 | |
| β-strand | 86 | 1 | 5 |
| α-helix | 87-88 | 2 | |
| α-helix | 89-91 | 3 | |
| β-strand | 93 | 1 | 6 |
| β-strand | 96 | 1 | 6 |
| β-strand | 98 | 1 | 5 |
| β-strand | 100-103 | 4 | 4 |
| α-helix | 107-109 | 3 | |
| β-strand | 115 | 1 | 2 |
| β-strand | 119-122 | 4 | 4 |
| α-helix | 124-130 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-10 | 2 | 7 |
| β-strand | 12 | 1 | 8 |
| α-helix | 21-26 | 6 | |
| β-strand | 32-33 | 2 | 9 |
| α-helix | 34-35 | 2 | |
| α-helix | 36-40 | 5 | |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 50-62 | 13 | |
| α-helix | 65-68 | 4 | |
| α-helix | 73-79 | 7 | |
| α-helix | 83-85 | 3 | |
| β-strand | 86 | 1 | 10 |
| α-helix | 87-88 | 2 | |
| α-helix | 89-91 | 3 | |
| β-strand | 93 | 1 | 11 |
| β-strand | 96 | 1 | 11 |
| β-strand | 98 | 1 | 10 |
| β-strand | 100-103 | 4 | 9 |
| α-helix | 107-109 | 3 | |
| β-strand | 115 | 1 | 8 |
| β-strand | 119-122 | 4 | 9 |
| α-helix | 124-131 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-10 | 2 | 12 |
| β-strand | 12 | 1 | 13 |
| β-strand | 16 | 1 | 14 |
| α-helix | 22-27 | 6 | |
| β-strand | 32 | 1 | 15 |
| α-helix | 33-34 | 2 | |
| β-strand | 35 | 1 | 14 |
| α-helix | 36-42 | 7 | |
| β-strand | 46-47 | 2 | 12 |
| α-helix | 50-62 | 13 | |
| α-helix | 65-68 | 4 | |
| α-helix | 73-81 | 9 | |
| α-helix | 83-85 | 3 | |
| β-strand | 86 | 1 | 16 |
| α-helix | 87-88 | 2 | |
| α-helix | 89-91 | 3 | |
| β-strand | 93 | 1 | 17 |
| β-strand | 96 | 1 | 17 |
| β-strand | 98 | 1 | 16 |
| β-strand | 100-103 | 4 | 15 |
| β-strand | 115 | 1 | 13 |
| β-strand | 119-122 | 4 | 15 |
| α-helix | 124-132 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-10 | 2 | 18 |
| β-strand | 12 | 1 | 19 |
| β-strand | 16 | 1 | 20 |
| α-helix | 22-27 | 6 | |
| β-strand | 32 | 1 | 21 |
| β-strand | 35 | 1 | 20 |
| α-helix | 36-42 | 7 | |
| β-strand | 46-47 | 2 | 18 |
| α-helix | 50-62 | 13 | |
| α-helix | 65-68 | 4 | |
| α-helix | 73-81 | 9 | |
| α-helix | 83-85 | 3 | |
| β-strand | 86 | 1 | 22 |
| α-helix | 87-88 | 2 | |
| α-helix | 89-91 | 3 | |
| β-strand | 93 | 1 | 23 |
| β-strand | 96 | 1 | 23 |
| β-strand | 98 | 1 | 22 |
| β-strand | 100-103 | 4 | 21 |
| α-helix | 107-109 | 3 | |
| β-strand | 115 | 1 | 19 |
| β-strand | 119-122 | 4 | 21 |
| α-helix | 124-132 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Colicin E9 | A, B, C, D | protein | 134 | ESCHERICHIA COLI | P09883 (AlphaFold model) |
| 5'-d(*gp*cp*gp*ap*tp*cp*gp*cp)-3' | E, F, G, H, I, J, K, L | DNA | 8 |
>1V14_1 COLICIN E9 (chains A, B, C, D) MESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEE VSKDPELSKNLNPSNKSSVSKGYSPFTPKNQQVGGRKVYELHADKPISQGGEVYDMDNIR VTTPKRHIDIHRGK
>1V14_2 5'-D(*GP*CP*GP*AP*TP*CP*GP*CP)-3' (chains E, F, G, H, I, J, K, L) GCGATCGC
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 6 |
Structure-Based Analysis of the Metal-Dependent Mechanism of H-N-H Endonucleases. Mate, M.J., Kleanthous, C. J Biol Chem (2004) 279:34763. DOI 10.1074/JBC.M403719200 · PubMed
Other PDB entries of the same protein (UniProt P09883 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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