Crystal structure of a lambda integrase tetramer bound to a Holliday junction. Determined by X-ray diffraction at 4.4 Å resolution. Released 28 Jun 2005.
Explore 1Z1G in 3D Show helices and sheets RCSB PDB PDBe
1Z1G contains 76 α-helices and 47 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 | 16-18 | 3 | 1 |
| β-strand | 24-27 | 4 | 1 |
| β-strand | 34-36 | 3 | 1 |
| α-helix | 41-54 | 14 | |
| α-helix | 66-69 | 4 | |
| α-helix | 76-89 | 14 | |
| α-helix | 94-110 | 17 | |
| α-helix | 116-118 | 3 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-167 | 3 | |
| α-helix | 170-172 | 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 | 2 |
| α-helix | 221-223 | 3 | |
| β-strand | 224-225 | 2 | 3 |
| β-strand | 228-232 | 5 | 3 |
| β-strand | 239-243 | 5 | 3 |
| β-strand | 247-248 | 2 | 4 |
| β-strand | 253-254 | 2 | 4 |
| α-helix | 255-265 | 11 | |
| β-strand | 270 | 1 | 2 |
| α-helix | 279-281 | 3 | |
| 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 |
|---|---|---|---|
| β-strand | 16-18 | 3 | 6 |
| β-strand | 24-27 | 4 | 6 |
| β-strand | 34-36 | 3 | 6 |
| α-helix | 41-54 | 14 | |
| β-strand | 75 | 1 | 7 |
| α-helix | 76-89 | 14 | |
| α-helix | 94-110 | 17 | |
| β-strand | 115 | 1 | 7 |
| α-helix | 116-118 | 3 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-167 | 3 | |
| α-helix | 169-171 | 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 | 8 |
| α-helix | 221-223 | 3 | |
| β-strand | 224-225 | 2 | 5 |
| β-strand | 228-232 | 5 | 5 |
| β-strand | 239-243 | 5 | 5 |
| β-strand | 247-248 | 2 | 9 |
| β-strand | 253-254 | 2 | 9 |
| α-helix | 255-265 | 11 | |
| β-strand | 270 | 1 | 8 |
| α-helix | 279-281 | 3 | |
| α-helix | 282-296 | 15 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-321 | 13 | |
| α-helix | 324-331 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-18 | 3 | 10 |
| β-strand | 24-27 | 4 | 10 |
| β-strand | 34-36 | 3 | 10 |
| α-helix | 41-54 | 14 | |
| α-helix | 64-69 | 6 | |
| α-helix | 76-89 | 14 | |
| α-helix | 94-110 | 17 | |
| α-helix | 116-118 | 3 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-167 | 3 | |
| α-helix | 169-172 | 4 | |
| α-helix | 182-191 | 10 | |
| α-helix | 197-209 | 13 | |
| α-helix | 213-216 | 4 | |
| β-strand | 220 | 1 | 11 |
| α-helix | 221-223 | 3 | |
| β-strand | 224-225 | 2 | 12 |
| β-strand | 228-232 | 5 | 12 |
| β-strand | 239-243 | 5 | 12 |
| β-strand | 247-248 | 2 | 13 |
| β-strand | 253-254 | 2 | 13 |
| α-helix | 255-265 | 11 | |
| β-strand | 270 | 1 | 11 |
| α-helix | 282-296 | 15 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-321 | 13 | |
| α-helix | 324-330 | 7 | |
| β-strand | 352 | 1 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-18 | 3 | 15 |
| β-strand | 24-27 | 4 | 15 |
| β-strand | 34-36 | 3 | 15 |
| α-helix | 41-54 | 14 | |
| β-strand | 75 | 1 | 16 |
| α-helix | 76-89 | 14 | |
| α-helix | 94-110 | 17 | |
| β-strand | 115 | 1 | 16 |
| α-helix | 116-118 | 3 | |
| α-helix | 121-133 | 13 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-167 | 3 | |
| α-helix | 170-172 | 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 | 17 |
| α-helix | 221-223 | 3 | |
| β-strand | 224-225 | 2 | 14 |
| β-strand | 228-232 | 5 | 14 |
| β-strand | 239-243 | 5 | 14 |
| β-strand | 247-248 | 2 | 18 |
| β-strand | 253-254 | 2 | 18 |
| α-helix | 255-265 | 11 | |
| β-strand | 270 | 1 | 17 |
| α-helix | 279-281 | 3 | |
| α-helix | 282-296 | 15 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-321 | 13 | |
| α-helix | 324-330 | 7 | |
| β-strand | 351-352 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 29-MER | I | DNA | 29 | ||
| 29-MER | J | DNA | 29 | ||
| 29-MER | K | DNA | 29 | ||
| 29-MER | L | DNA | 29 | ||
| 5'-d(*ap*cp*ap*gp*gp*tp*cp*ap*cp*tp*ap*tp*cp*ap*gp*tp*cp*ap*ap*ap*ap*tp*ap*cp*c)-3' | E, G | DNA | 25 | ||
| 25-MER | F, H | DNA | 25 | ||
| Integrase | A, B, C, D | protein | 356 | Enterobacteria phage lambda | P03700 |
>1Z1G_1 29-MER (chains I) AACTCTGCTTTTTACAACAAAGTTGGATC
>1Z1G_2 29-MER (chains J) CGCTCAAGTTTATATTAAAAAGCAGAGTT
>1Z1G_3 29-MER (chains K) TTGCCAGCTTTATTATATAAACTTGAGCG
>1Z1G_4 29-MER (chains L) GATCCAACTTTGTTGAATAAAGCTGGCAA
>1Z1G_5 5'-D(*AP*CP*AP*GP*GP*TP*CP*AP*CP*TP*AP*TP*CP*AP*GP*TP*CP*AP*AP*AP*AP*TP*AP*CP*C)-3' (chains E, G) ACAGGTCACTATCAGTCAAAATACC
>1Z1G_6 25-MER (chains F, H) GGTATTTTGACTGATAGTGACCTGT
>1Z1G_7 Integrase (chains A, B, C, D) MGRRRSHERRDLPPNLYIRNNGYYCYRDPRTGKEFGLGRDRRIAITEAIQANIELFSGHK HKPLTARINSDNSVTLHSWLDRYEKILASRGIKQKTLINYMSKIKAIRRGLPDAPLEDIT TKEIAAMLNGYIDEGKAASAKLIRSTLSDAFREAIAEGHITTNHVAATRAAKSEVRRSRL TADEYLKIYQAAESSPCWLRLAMELAVVTGQRVGDLCEMKWSDIVDGYLYVEQSKTGVKI AIPTALHIDALGISMKETLDKCKEILGGETIIASTRREPLSSGTVSRYFMRARKASGLSF EGDPPTFHELRSLSARLYEKQISDKFAQHLLGHKSDTMASQFRDDRGREWDKIEIK
A structural basis for allosteric control of DNA recombination by lambda integrase. Biswas, T., Aihara, H., Radman-Livaja, M. et al. Nature (2005) 435:1059-1066. DOI 10.1038/nature03657 · PubMed
Other PDB entries of the same protein (UniProt P03700), best resolution first:
MolViewer shows 1Z1G directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.