Crystal structure of yeast primase catalytic subunit. Determined by X-ray diffraction at 1.6 Å resolution. Released 10 Sept 2014.
Explore 4MM2 in 3D Show helices and sheets RCSB PDB PDBe
4MM2 contains 51 α-helices and 30 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 | 9-11 | 3 | |
| α-helix | 12-21 | 10 | |
| α-helix | 25-33 | 9 | |
| β-strand | 39 | 1 | 1 |
| α-helix | 40-43 | 4 | |
| β-strand | 45-50 | 6 | 2 |
| β-strand | 56-60 | 5 | 2 |
| α-helix | 65-75 | 11 | |
| β-strand | 79-86 | 8 | 2 |
| α-helix | 90-92 | 3 | |
| β-strand | 103-105 | 3 | 2 |
| β-strand | 108-113 | 6 | 3 |
| α-helix | 114-117 | 4 | |
| α-helix | 131-146 | 16 | |
| α-helix | 147-152 | 6 | |
| β-strand | 157-161 | 5 | 3 |
| β-strand | 166-171 | 6 | 3 |
| α-helix | 174-177 | 4 | |
| α-helix | 181-191 | 11 | |
| α-helix | 211-224 | 14 | |
| α-helix | 225-232 | 8 | |
| α-helix | 238-244 | 7 | |
| α-helix | 246-248 | 3 | |
| α-helix | 252-264 | 13 | |
| α-helix | 270-285 | 16 | |
| α-helix | 290-309 | 20 | |
| β-strand | 313 | 1 | 3 |
| α-helix | 315-319 | 5 | |
| β-strand | 325-326 | 2 | 2 |
| α-helix | 327 | 1 | |
| α-helix | 330 | 1 | |
| β-strand | 331 | 1 | 4 |
| α-helix | 332 | 1 | |
| β-strand | 337 | 1 | 5 |
| β-strand | 338 | 1 | 4 |
| β-strand | 341-342 | 2 | 3 |
| α-helix | 348-350 | 3 | |
| α-helix | 352 | 1 | |
| β-strand | 353 | 1 | 5 |
| α-helix | 354-363 | 10 | |
| α-helix | 373-401 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-21 | 10 | |
| α-helix | 25-33 | 9 | |
| β-strand | 39 | 1 | 1 |
| α-helix | 40-43 | 4 | |
| β-strand | 45-50 | 6 | 6 |
| β-strand | 56-60 | 5 | 6 |
| α-helix | 65-75 | 11 | |
| β-strand | 79-86 | 8 | 6 |
| α-helix | 90-92 | 3 | |
| β-strand | 103-105 | 3 | 6 |
| β-strand | 108-113 | 6 | 7 |
| α-helix | 114-117 | 4 | |
| α-helix | 131-146 | 16 | |
| α-helix | 147-152 | 6 | |
| β-strand | 157-161 | 5 | 7 |
| β-strand | 166-171 | 6 | 7 |
| α-helix | 174-177 | 4 | |
| α-helix | 181-191 | 11 | |
| α-helix | 211-224 | 14 | |
| α-helix | 225-232 | 8 | |
| α-helix | 238-244 | 7 | |
| α-helix | 246-248 | 3 | |
| α-helix | 252-264 | 13 | |
| α-helix | 270-285 | 16 | |
| α-helix | 290-309 | 20 | |
| β-strand | 313 | 1 | 7 |
| α-helix | 315-319 | 5 | |
| β-strand | 325-326 | 2 | 6 |
| α-helix | 327 | 1 | |
| α-helix | 330 | 1 | |
| β-strand | 331 | 1 | 8 |
| α-helix | 332 | 1 | |
| β-strand | 337 | 1 | 9 |
| β-strand | 338 | 1 | 8 |
| β-strand | 341-342 | 2 | 7 |
| α-helix | 348-350 | 3 | |
| α-helix | 352 | 1 | |
| β-strand | 353 | 1 | 9 |
| α-helix | 354-363 | 10 | |
| α-helix | 373-401 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA primase small subunit | A, B | protein | 414 | Saccharomyces cerevisiae | P10363 (AlphaFold model) |
>4MM2_1 DNA primase small subunit (chains A, B) GAMGSMTNSVKTNGPSSSDMEYYYKSLYPFKHIFNWLNHSPKPSRDMINREFAMAFRSGA YKRYNSFNSVQDFKAQIEKANPDRFEIGAIYNKPPRERDTLLKSELKALEKELVFDIDMD DYDAFRTCCSGAQVCSKCWKFISLAMKITNTALREDFGYKDFIWVFSGRRGAHCWVSDKR ARALTDVQRRNVLDYVNVIRDRNTDKRLALKRPYHPHLARSLEQLKPFFVSIMLEEQNPW EDDQHAIQTLLPALYDKQLIDSLKKYWLDNPRRSSKEKWNDIDQIATSLFKGPKQDSHII KLRECKEDLVLMTLYPKLDVEVTKQTIHLLKAPFCIHPATGNVCVPIDESFAPEKAPKLI DLQTEMEKNNDVSLTALQPFINQFQAYVSSLLKNELGSVKREREDDDEPASLDF
Crystal structure of yeast primase catalytic subunit. Park, K.R., An, J.Y., Lee, Y. et al. To be published.
Other PDB entries of the same protein (UniProt P10363 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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