Crystal structure of the Pri1 subunit of human primase bound to vidarabine triphosphate. Determined by X-ray diffraction at 2.35 Å resolution. Released 11 Sept 2019.
Explore 6R4T in 3D Show helices and sheets RCSB PDB PDBe
6R4T contains 56 α-helices and 26 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 | 9-19 | 11 | |
| α-helix | 23-31 | 9 | |
| α-helix | 32-34 | 3 | |
| β-strand | 43-48 | 6 | 1 |
| α-helix | 50-52 | 3 | |
| β-strand | 54-58 | 5 | 1 |
| α-helix | 63-73 | 11 | |
| β-strand | 77-84 | 8 | 1 |
| α-helix | 88-90 | 3 | |
| α-helix | 95 | 1 | |
| β-strand | 101-103 | 3 | 1 |
| β-strand | 106-111 | 6 | 2 |
| α-helix | 112-118 | 7 | |
| α-helix | 133-144 | 12 | |
| α-helix | 145-149 | 5 | |
| β-strand | 155-159 | 5 | 2 |
| β-strand | 164-169 | 6 | 2 |
| α-helix | 172-175 | 4 | |
| α-helix | 179-189 | 11 | |
| α-helix | 208-209 | 2 | |
| α-helix | 210-223 | 14 | |
| α-helix | 224-230 | 7 | |
| α-helix | 237-244 | 8 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-261 | 10 | |
| α-helix | 265-278 | 14 | |
| α-helix | 291-301 | 11 | |
| α-helix | 307-311 | 5 | |
| β-strand | 317-318 | 2 | 1 |
| α-helix | 319 | 1 | |
| β-strand | 323 | 1 | 3 |
| β-strand | 329 | 1 | 4 |
| β-strand | 330 | 1 | 3 |
| β-strand | 333 | 1 | 2 |
| α-helix | 336-338 | 3 | |
| α-helix | 344-346 | 3 | |
| α-helix | 348 | 1 | |
| β-strand | 349 | 1 | 4 |
| α-helix | 350-358 | 9 | |
| α-helix | 383-385 | 3 | |
| α-helix | 389-406 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 9-19 | 11 | |
| α-helix | 23-31 | 9 | |
| α-helix | 32-34 | 3 | |
| β-strand | 43-48 | 6 | 5 |
| α-helix | 50-52 | 3 | |
| β-strand | 54-58 | 5 | 5 |
| α-helix | 63-73 | 11 | |
| β-strand | 77-84 | 8 | 5 |
| α-helix | 88-90 | 3 | |
| α-helix | 95 | 1 | |
| β-strand | 101-103 | 3 | 5 |
| β-strand | 106-111 | 6 | 6 |
| α-helix | 112-118 | 7 | |
| α-helix | 129-144 | 16 | |
| α-helix | 145-149 | 5 | |
| β-strand | 155-159 | 5 | 6 |
| β-strand | 164-169 | 6 | 6 |
| α-helix | 179-189 | 11 | |
| α-helix | 208-209 | 2 | |
| α-helix | 210-223 | 14 | |
| α-helix | 224-230 | 7 | |
| α-helix | 237-244 | 8 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-261 | 10 | |
| α-helix | 265-278 | 14 | |
| α-helix | 291-301 | 11 | |
| α-helix | 307-311 | 5 | |
| β-strand | 317-318 | 2 | 5 |
| α-helix | 319 | 1 | |
| β-strand | 323 | 1 | 7 |
| β-strand | 329 | 1 | 8 |
| β-strand | 330 | 1 | 7 |
| β-strand | 333 | 1 | 6 |
| α-helix | 336-338 | 3 | |
| α-helix | 344-346 | 3 | |
| α-helix | 348 | 1 | |
| β-strand | 349 | 1 | 8 |
| α-helix | 350-357 | 8 | |
| α-helix | 383-385 | 3 | |
| α-helix | 389-404 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA primase small subunit | A, D | protein | 410 | Homo sapiens | P49642 (AlphaFold model) |
>6R4T_1 DNA primase small subunit (chains A, D) GTSMETFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRY QSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDD VRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKL SSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENK ESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIM LQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICREL DAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
| MN | Manganese (II) ion | Mn | 2 |
| HEJ | 9-{5-O-[(S)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}phosphoryl]-beta-D… | C10 H16 N5 O13 P3 | 2 |
Water and common crystallization additives (EDO) are not listed.
Structural Basis for Inhibition of Human Primase by Arabinofuranosyl Nucleoside Analogues Fludarabine and Vidarabine. Holzer, S., Rzechorzek, N.J., Short, I.R. et al. ACS Chem Biol (2019) 14:1904-1912. DOI 10.1021/acschembio.9b00367 · PubMed
Other PDB entries of the same protein (UniProt P49642 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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