Pre-catalytic quaternary complex of DNA Polymerase Lambda with bound complementary DSB substrate and incoming dUMPNPP. Determined by X-ray diffraction at 1.8 Å resolution. Released 16 Mar 2022.
Explore 7M0D in 3D Show helices and sheets RCSB PDB PDBe
7M0D contains 50 α-helices and 24 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 | 240-242 | 3 | |
| α-helix | 245-248 | 4 | |
| α-helix | 254-269 | 16 | |
| α-helix | 273-288 | 16 | |
| α-helix | 296-301 | 6 | |
| α-helix | 307-319 | 13 | |
| α-helix | 323-327 | 5 | |
| α-helix | 332-339 | 8 | |
| α-helix | 346-354 | 9 | |
| α-helix | 360-366 | 7 | |
| α-helix | 371-378 | 8 | |
| α-helix | 380-384 | 5 | |
| α-helix | 386 | 1 | |
| β-strand | 387-388 | 2 | 1 |
| α-helix | 389-404 | 16 | |
| 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 | 443-453 | 11 | |
| β-strand | 457-464 | 8 | 2 |
| β-strand | 471-478 | 8 | 2 |
| α-helix | 484-485 | 2 | |
| β-strand | 486-493 | 8 | 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 |
| α-helix | 535-536 | 2 | |
| β-strand | 537-538 | 2 | 4 |
| β-strand | 544-546 | 3 | 4 |
| α-helix | 549 | 1 | |
| β-strand | 550-551 | 2 | 3 |
| α-helix | 552 | 1 | |
| α-helix | 556-562 | 7 | |
| α-helix | 570-573 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 240-242 | 3 | |
| α-helix | 245-248 | 4 | |
| α-helix | 254-269 | 16 | |
| α-helix | 273-288 | 16 | |
| α-helix | 296-301 | 6 | |
| α-helix | 307-319 | 13 | |
| α-helix | 323-327 | 5 | |
| α-helix | 332-339 | 8 | |
| α-helix | 346-354 | 9 | |
| α-helix | 360-366 | 7 | |
| α-helix | 371-378 | 8 | |
| α-helix | 380-384 | 5 | |
| α-helix | 386 | 1 | |
| β-strand | 387-388 | 2 | 5 |
| α-helix | 389-404 | 16 | |
| β-strand | 411-414 | 4 | 6 |
| α-helix | 416-419 | 4 | |
| β-strand | 424-425 | 2 | 5 |
| β-strand | 428-433 | 6 | 6 |
| α-helix | 443-453 | 11 | |
| β-strand | 457-467 | 11 | 6 |
| β-strand | 470-478 | 9 | 6 |
| α-helix | 484-485 | 2 | |
| β-strand | 486-493 | 8 | 6 |
| α-helix | 496-498 | 3 | |
| α-helix | 499-507 | 9 | |
| α-helix | 510-522 | 13 | |
| β-strand | 525-527 | 3 | 7 |
| β-strand | 532-534 | 3 | 7 |
| α-helix | 535-536 | 2 | |
| β-strand | 537-538 | 2 | 8 |
| β-strand | 544-546 | 3 | 8 |
| α-helix | 549 | 1 | |
| β-strand | 550-551 | 2 | 7 |
| α-helix | 552 | 1 | |
| α-helix | 556-562 | 7 | |
| α-helix | 570-572 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase lambda | A, B | protein | 346 | Homo sapiens | Q9UGP5 (AlphaFold model) |
| DNA (5'-d(*cp*gp*gp*cp*ap*gp*c)-3') | G, K | DNA | 7 | synthetic construct | |
| DNA (5'-d(*cp*ap*gp*tp*gp*c)-3') | F, J | DNA | 6 | synthetic construct | |
| DNA (5'-d(p*gp*cp*cp*g)-3') | H, L | DNA | 4 | synthetic construct | |
| DNA (5'-d(*ap*cp*tp*g)-3') | E, I | DNA | 4 | synthetic construct |
>7M0D_1 DNA polymerase lambda (chains A, B) GSAAAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSF HKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTA QMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSG LLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQ QQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSE HALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
>7M0D_2 DNA (5'-D(*CP*GP*GP*CP*AP*GP*C)-3') (chains G, K) CGGCAGC
>7M0D_3 DNA (5'-D(*CP*AP*GP*TP*GP*C)-3') (chains F, J) CAGTGC
>7M0D_4 DNA (5'-D(P*GP*CP*CP*G)-3') (chains H, L) GCCG
>7M0D_5 DNA (5'-D(*AP*CP*TP*G)-3') (chains E, I) ACTG
| ID | Name | Formula | Copies |
|---|---|---|---|
| DUP | 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate | C9 H16 N3 O13 P3 | 2 |
| MG | Magnesium ion | Mg | 2 |
| CIT | Citric acid | C6 H8 O7 | 2 |
Water and common crystallization additives (K, NA, FMT, CL, EDO, TRS) are not listed.
Analysis of diverse double-strand break synapsis with Pol lambda reveals basis for unique substrate specificity in nonhomologous end-joining. Kaminski, A.M., Chiruvella, K.K., Ramsden, D.A. et al. Nat Commun (2022) 13:3806-3806. DOI 10.1038/s41467-022-31278-4 · 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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