Toroidal structure of lambda exonuclease determined at 2.4 Å. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Mar 1998.
Explore 1AVQ in 3D Show helices and sheets RCSB PDB PDBe
1AVQ contains 37 α-helices and 24 β-strands across 3 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 | 3-10 | 8 | |
| α-helix | 14-16 | 3 | |
| α-helix | 22-26 | 5 | |
| β-strand | 32-33 | 2 | 1 |
| α-helix | 37-39 | 3 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-67 | 16 | |
| α-helix | 75-96 | 22 | |
| β-strand | 100-101 | 2 | 2 |
| β-strand | 106-107 | 2 | 1 |
| β-strand | 114-116 | 3 | 1 |
| β-strand | 120-122 | 3 | 2 |
| β-strand | 127-131 | 5 | 2 |
| α-helix | 136-145 | 10 | |
| α-helix | 147-149 | 3 | |
| α-helix | 152-165 | 14 | |
| β-strand | 169-175 | 7 | 2 |
| β-strand | 184-190 | 7 | 2 |
| α-helix | 193-216 | 24 | |
| α-helix | 223-225 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-10 | 8 | |
| α-helix | 14-16 | 3 | |
| α-helix | 22-26 | 5 | |
| β-strand | 32-33 | 2 | 3 |
| α-helix | 37-41 | 5 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-67 | 16 | |
| α-helix | 75-96 | 22 | |
| β-strand | 100-101 | 2 | 4 |
| β-strand | 106-107 | 2 | 3 |
| β-strand | 114-116 | 3 | 3 |
| β-strand | 120-122 | 3 | 4 |
| β-strand | 126-131 | 6 | 4 |
| α-helix | 136-145 | 10 | |
| α-helix | 146-149 | 4 | |
| α-helix | 152-165 | 14 | |
| β-strand | 169-175 | 7 | 4 |
| β-strand | 184-190 | 7 | 4 |
| α-helix | 193-216 | 24 | |
| α-helix | 223-225 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-10 | 8 | |
| α-helix | 14-16 | 3 | |
| α-helix | 22-26 | 5 | |
| β-strand | 32-33 | 2 | 5 |
| α-helix | 34-36 | 3 | |
| α-helix | 38-41 | 4 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-67 | 16 | |
| α-helix | 75-96 | 22 | |
| β-strand | 100-101 | 2 | 6 |
| β-strand | 106-107 | 2 | 5 |
| β-strand | 114-116 | 3 | 5 |
| β-strand | 120-122 | 3 | 6 |
| β-strand | 127-131 | 5 | 6 |
| α-helix | 136-145 | 10 | |
| α-helix | 146-148 | 3 | |
| α-helix | 152-165 | 14 | |
| β-strand | 169-175 | 7 | 6 |
| β-strand | 184-190 | 7 | 6 |
| α-helix | 193-217 | 25 | |
| α-helix | 223-225 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lambda exonuclease | A, B, C | protein | 228 | Enterobacteria phage lambda | P03697 |
>1AVQ_1 LAMBDA EXONUCLEASE (chains A, B, C) SHMTPDIILQRTGIDVRAVEQGDDAWHKLRLGVITASEVHNVIAKPRSGKKWPDMKMSYF HTLLAEVCTGVAPEVNAKALAWGKQYENDARTLFEFTSGVNVTESPIIYRDESMRTACSP DGLCSDGNGLELKCPFTSRDFMKFRLGGFEAIKSAYMAQVQYSMWVTRKNAWYFANYDPR MKREGLHYVVIERDEKYMASFDEIVPEFIEKMDEALAEIGFVFGEQWR
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 3 |
Water and common crystallization additives (ACT) are not listed.
Toroidal structure of lambda-exonuclease. Kovall, R., Matthews, B.W. Science (1997) 277:1824-1827. DOI 10.1126/science.277.5333.1824 · PubMed
Other PDB entries of the same protein (UniProt P03697), best resolution first:
MolViewer shows 1AVQ 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.