Crystal structure of UvrD-DNA-ADPMgF3 ternary complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 9 Jan 2007.
Explore 2IS6 in 3D Show helices and sheets RCSB PDB PDBe
2IS6 contains 85 α-helices and 46 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 | 3-7 | 5 | |
| α-helix | 12-18 | 7 | |
| α-helix | 20-21 | 2 | |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 35-48 | 14 | |
| α-helix | 54-56 | 3 | |
| β-strand | 57-61 | 5 | 1 |
| α-helix | 64-78 | 15 | |
| β-strand | 86-89 | 4 | 1 |
| α-helix | 90-100 | 11 | |
| β-strand | 112-114 | 3 | 2 |
| α-helix | 116-129 | 14 | |
| α-helix | 139-151 | 13 | |
| α-helix | 165-184 | 20 | |
| β-strand | 186-188 | 3 | 2 |
| α-helix | 189-202 | 14 | |
| α-helix | 204-213 | 10 | |
| β-strand | 216-219 | 4 | 1 |
| α-helix | 222-224 | 3 | |
| α-helix | 227-237 | 11 | |
| β-strand | 242-247 | 6 | 1 |
| α-helix | 249-251 | 3 | |
| α-helix | 255-257 | 3 | |
| α-helix | 262-270 | 9 | |
| β-strand | 275-278 | 4 | 1 |
| β-strand | 281 | 1 | 3 |
| α-helix | 287-298 | 12 | |
| β-strand | 309 | 1 | 3 |
| α-helix | 317 | 1 | |
| β-strand | 318-325 | 8 | 4 |
| α-helix | 326-342 | 17 | |
| α-helix | 347-349 | 3 | |
| β-strand | 350-354 | 5 | 4 |
| α-helix | 357-359 | 3 | |
| α-helix | 360-369 | 10 | |
| β-strand | 374-376 | 3 | 4 |
| α-helix | 382-384 | 3 | |
| α-helix | 386-399 | 14 | |
| α-helix | 404-410 | 7 | |
| α-helix | 420-433 | 14 | |
| α-helix | 437-445 | 9 | |
| α-helix | 452-471 | 20 | |
| α-helix | 477-487 | 11 | |
| α-helix | 490-495 | 6 | |
| α-helix | 500-518 | 19 | |
| α-helix | 530-540 | 11 | |
| α-helix | 542-544 | 3 | |
| β-strand | 554-558 | 5 | 4 |
| α-helix | 559-562 | 4 | |
| β-strand | 567-572 | 6 | 4 |
| β-strand | 576 | 1 | 5 |
| β-strand | 578 | 1 | 6 |
| β-strand | 582 | 1 | 6 |
| α-helix | 583-586 | 4 | |
| α-helix | 592-603 | 12 | |
| β-strand | 606-617 | 12 | 4 |
| β-strand | 618-620 | 3 | 7 |
| β-strand | 623-625 | 3 | 7 |
| α-helix | 627-628 | 2 | |
| β-strand | 629 | 1 | 5 |
| α-helix | 630 | 1 | |
| α-helix | 631-635 | 5 | |
| α-helix | 638-640 | 3 | |
| β-strand | 641-643 | 3 | 4 |
| α-helix | 646-648 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 | |
| α-helix | 12-18 | 7 | |
| β-strand | 25-28 | 4 | 8 |
| α-helix | 35-48 | 14 | |
| α-helix | 54-56 | 3 | |
| β-strand | 57-61 | 5 | 8 |
| α-helix | 64-78 | 15 | |
| β-strand | 86-89 | 4 | 8 |
| α-helix | 90-100 | 11 | |
| α-helix | 102-105 | 4 | |
| β-strand | 112-114 | 3 | 9 |
| α-helix | 116-129 | 14 | |
| α-helix | 139-151 | 13 | |
| α-helix | 165-184 | 20 | |
| β-strand | 186-188 | 3 | 9 |
| α-helix | 189-202 | 14 | |
| α-helix | 204-213 | 10 | |
| β-strand | 216-219 | 4 | 8 |
| α-helix | 222-224 | 3 | |
| α-helix | 227-237 | 11 | |
| β-strand | 242-247 | 6 | 8 |
| α-helix | 249-251 | 3 | |
| α-helix | 255-257 | 3 | |
| α-helix | 262-270 | 9 | |
| β-strand | 275-278 | 4 | 8 |
| β-strand | 281 | 1 | 10 |
| α-helix | 287-297 | 11 | |
| β-strand | 309 | 1 | 10 |
| α-helix | 317 | 1 | |
| β-strand | 318-323 | 6 | 11 |
| α-helix | 326-342 | 17 | |
| α-helix | 347-349 | 3 | |
| β-strand | 350-354 | 5 | 11 |
| α-helix | 357-359 | 3 | |
| α-helix | 360-369 | 10 | |
| β-strand | 374-376 | 3 | 11 |
| α-helix | 382-384 | 3 | |
| α-helix | 386-399 | 14 | |
| α-helix | 404-410 | 7 | |
| α-helix | 420-433 | 14 | |
| α-helix | 437-446 | 10 | |
| α-helix | 452-471 | 20 | |
| α-helix | 477-487 | 11 | |
| α-helix | 490-496 | 7 | |
| α-helix | 502-517 | 16 | |
| α-helix | 530-540 | 11 | |
| α-helix | 542-544 | 3 | |
| α-helix | 547-548 | 2 | |
| β-strand | 554-558 | 5 | 11 |
| α-helix | 559-562 | 4 | |
| β-strand | 567-572 | 6 | 11 |
| β-strand | 576 | 1 | 12 |
| β-strand | 578-579 | 2 | 13 |
| β-strand | 582 | 1 | 13 |
| α-helix | 583-586 | 4 | |
| α-helix | 591-603 | 13 | |
| β-strand | 606-615 | 10 | 11 |
| β-strand | 618-620 | 3 | 14 |
| β-strand | 623-625 | 3 | 14 |
| α-helix | 627-628 | 2 | |
| β-strand | 629 | 1 | 12 |
| α-helix | 630 | 1 | |
| α-helix | 631-635 | 5 | |
| β-strand | 641-643 | 3 | 11 |
| α-helix | 644-645 | 2 | |
| α-helix | 651-653 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*cp*gp*ap*gp*cp*ap*cp*tp*gp*cp*ap*gp*tp*gp*cp*tp*cp*gp*tp*tp*gp*tp*tp*ap*t)-3' | C, D | DNA | 25 | ||
| DNA helicase II | A, B | protein | 680 | Escherichia coli | P03018 (AlphaFold model) |
>2IS6_1 5'-D(*CP*GP*AP*GP*CP*AP*CP*TP*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*TP*TP*GP*TP*TP*AP*T)-3' (chains C, D) CGAGCACTGCAGTGCTCGTTGTTAT
>2IS6_2 DNA helicase II (chains A, B) MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAV TFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQL RLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEA CDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDT GKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENN NGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQS RVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIVNRNDDAAFERVVNTPTRGIGD RTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQ TDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAAL EAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAY VGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMG TPMVENDSGYKLGQRVRHAK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| MGF | Trifluoromagnesate | F3 Mg | 2 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (GOL) are not listed.
UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Lee, J.Y., Yang, W. Cell (2006) 127:1349-1360. DOI 10.1016/j.cell.2006.10.049 · PubMed
Other PDB entries of the same protein (UniProt P03018 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2IS6 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.