Na in the active site of DNA Polymerase lambda. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 May 2007.
Explore 2PFN in 3D Show helices and sheets RCSB PDB PDBe
2PFN contains 19 α-helices and 12 β-strands across 1 chain. 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 | 254-269 | 16 | |
| α-helix | 273-287 | 15 | |
| α-helix | 296-300 | 5 | |
| α-helix | 307-317 | 11 | |
| α-helix | 323-327 | 5 | |
| α-helix | 331-339 | 9 | |
| α-helix | 346-354 | 9 | |
| α-helix | 360-366 | 7 | |
| α-helix | 371-378 | 8 | |
| α-helix | 380-384 | 5 | |
| β-strand | 387-388 | 2 | 1 |
| α-helix | 389-406 | 18 | |
| β-strand | 411-414 | 4 | 2 |
| α-helix | 416-419 | 4 | |
| β-strand | 424-425 | 2 | 1 |
| β-strand | 428-433 | 6 | 2 |
| α-helix | 444-453 | 10 | |
| β-strand | 457-462 | 6 | 2 |
| β-strand | 472-477 | 6 | 2 |
| β-strand | 487-493 | 7 | 2 |
| α-helix | 496-498 | 3 | |
| α-helix | 499-507 | 9 | |
| α-helix | 510-522 | 13 | |
| β-strand | 525-527 | 3 | 3 |
| β-strand | 532-534 | 3 | 3 |
| β-strand | 538 | 1 | 4 |
| β-strand | 544 | 1 | 4 |
| β-strand | 549-551 | 3 | 3 |
| α-helix | 552 | 1 | |
| α-helix | 556-562 | 7 | |
| α-helix | 570-573 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Template | T | DNA | 11 | ||
| Primer | P | DNA | 6 | ||
| Downstream Primer | D | DNA | 4 | ||
| DNA polymerase lambda | A | protein | 335 | Homo sapiens | Q9UGP5 (AlphaFold model) |
>2PFN_1 Template (chains T) CGGCAGTACTG
>2PFN_2 Primer (chains P) CAGTAC
>2PFN_3 Downstream Primer (chains D) GCCG
>2PFN_4 DNA polymerase lambda (chains A) MAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEAC SIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSL EDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLP GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNT HGAKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
| ID | Name | Formula | Copies |
|---|---|---|---|
| DUP | 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate | C9 H16 N3 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (NA) are not listed.
Role of the catalytic metal during polymerization by DNA polymerase lambda. Garcia-Diaz, M., Bebenek, K., Krahn, J.M. et al. DNA Repair (Amst) (2007) 6:1333-1340. DOI 10.1016/j.dnarep.2007.03.005 · PubMed
Other PDB entries of the same protein (UniProt Q9UGP5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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