Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA. Determined by X-ray diffraction at 2.95 Å resolution. Released 12 Aug 2003.
Explore 1P7D in 3D Show helices and sheets RCSB PDB PDBe
1P7D contains 34 α-helices and 19 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 | 76-87 | 12 | |
| α-helix | 94-110 | 17 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 169-172 | 4 | |
| α-helix | 177-180 | 4 | |
| α-helix | 182-191 | 10 | |
| α-helix | 192-194 | 3 | |
| α-helix | 197-209 | 13 | |
| α-helix | 213-216 | 4 | |
| β-strand | 220 | 1 | 1 |
| α-helix | 221-223 | 3 | |
| β-strand | 224 | 1 | 2 |
| β-strand | 228-232 | 5 | 2 |
| β-strand | 239-243 | 5 | 2 |
| β-strand | 247-248 | 2 | 3 |
| β-strand | 253-254 | 2 | 3 |
| α-helix | 255-261 | 7 | |
| α-helix | 262-266 | 5 | |
| β-strand | 270 | 1 | 1 |
| β-strand | 273 | 1 | 4 |
| β-strand | 279 | 1 | 4 |
| α-helix | 282-296 | 15 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-321 | 13 | |
| α-helix | 324-331 | 8 | |
| β-strand | 351-352 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 76-88 | 13 | |
| α-helix | 94-110 | 17 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 169-172 | 4 | |
| α-helix | 177-179 | 3 | |
| α-helix | 182-191 | 10 | |
| α-helix | 192-194 | 3 | |
| α-helix | 197-209 | 13 | |
| α-helix | 213-216 | 4 | |
| β-strand | 220 | 1 | 6 |
| α-helix | 221-223 | 3 | |
| β-strand | 224 | 1 | 5 |
| β-strand | 228-232 | 5 | 5 |
| β-strand | 239-243 | 5 | 5 |
| β-strand | 247-248 | 2 | 7 |
| β-strand | 253-254 | 2 | 7 |
| α-helix | 255-261 | 7 | |
| α-helix | 262-266 | 5 | |
| β-strand | 270 | 1 | 6 |
| β-strand | 273 | 1 | 8 |
| β-strand | 279 | 1 | 8 |
| α-helix | 282-296 | 15 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-321 | 13 | |
| α-helix | 324-331 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*cp*ap*ap*tp*gp*cp*cp*ap*ap*cp*tp*tp*t)-3' | C, E | DNA | 13 | ||
| 26-MER | D, F | DNA | 26 | ||
| Integrase | A, B | protein | 283 | Enterobacteria phage lambda | P03700 |
>1P7D_1 5'-D(*CP*AP*AP*TP*GP*CP*CP*AP*AP*CP*TP*TP*T)-3' (chains C, E) CAATGCCAACTTT
>1P7D_2 26-MER (chains D, F) TTTGCGAAGCAAAAAAGTTGGCATTG
>1P7D_3 Integrase (chains A, B) MTLHSWLDRYEKILASRGIKQKTLINYMSKIKAIRRGLPDAPLEDITTKEIAAMLNGYID EGKAASAKLIRSTLSDAFREAIAEGHITTNHVAATRAAKSEVRRSRLTADEYLKIYQAAE SSPCWLRLAMELAVVTGQRVGDLCEMKWSDIVDGYLYVEQSKTGVKIAIPTALHIDALGI SMKETLDKCKEILGGETIIASTRREPLSSGTVSRYFMRARKASGLSFEGDPPTFHELRSL SARLYEKQISDKFAQHLLGHKSDTMASQYRDDRGREWDKIEIK
A Conformational Switch Controls the DNA Cleavage Activity of Lambda Integrase. Aihara, H., Kwon, H.J., Nunes-Duby, S.E. et al. Mol Cell (2003) 12:187-198. DOI 10.1016/S1097-2765(03)00268-5 · PubMed
Other PDB entries of the same protein (UniProt P03700), best resolution first:
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