CRYSTAL STRUCTURE OF THE HUMAN RNA guanylyltransferase and 5'- phosphatase. Determined by X-ray diffraction at 1.6 Å resolution. Released 1 Nov 2005.
Explore 2C46 in 3D Show helices and sheets RCSB PDB PDBe
2C46 contains 64 α-helices and 24 β-strands across 4 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 | -4--2 | 3 | |
| α-helix | 5-7 | 3 | |
| β-strand | 16 | 1 | 1 |
| α-helix | 18-19 | 2 | |
| β-strand | 20 | 1 | 1 |
| β-strand | 24-27 | 4 | 1 |
| α-helix | 28-30 | 3 | |
| α-helix | 33-38 | 6 | |
| α-helix | 41-43 | 3 | |
| α-helix | 47-57 | 11 | |
| β-strand | 60-66 | 7 | 1 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 100-110 | 11 | |
| β-strand | 120-125 | 6 | 1 |
| α-helix | 131-143 | 13 | |
| α-helix | 149-159 | 11 | |
| α-helix | 167-177 | 11 | |
| α-helix | 180-182 | 3 | |
| α-helix | 183-190 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -4--2 | 3 | |
| α-helix | 5-7 | 3 | |
| β-strand | 16 | 1 | 2 |
| α-helix | 18-19 | 2 | |
| β-strand | 20 | 1 | 2 |
| β-strand | 24-27 | 4 | 2 |
| α-helix | 28-30 | 3 | |
| α-helix | 33-35 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 47-57 | 11 | |
| β-strand | 61-66 | 6 | 2 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-88 | 4 | 2 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-98 | 3 | |
| α-helix | 100-115 | 16 | |
| β-strand | 121-125 | 5 | 2 |
| α-helix | 131-145 | 15 | |
| α-helix | 149-159 | 11 | |
| α-helix | 167-177 | 11 | |
| α-helix | 180-182 | 3 | |
| α-helix | 183-190 | 8 | |
| α-helix | 191-193 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -4--2 | 3 | |
| α-helix | 5-7 | 3 | |
| β-strand | 16 | 1 | 3 |
| α-helix | 18-19 | 2 | |
| β-strand | 20 | 1 | 3 |
| β-strand | 24-27 | 4 | 3 |
| α-helix | 28-30 | 3 | |
| α-helix | 33-38 | 6 | |
| α-helix | 41-43 | 3 | |
| α-helix | 47-56 | 10 | |
| β-strand | 61-66 | 6 | 3 |
| α-helix | 76-80 | 5 | |
| β-strand | 85-88 | 4 | 3 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 100-111 | 12 | |
| β-strand | 121-125 | 5 | 3 |
| α-helix | 131-145 | 15 | |
| α-helix | 149-159 | 11 | |
| α-helix | 167-177 | 11 | |
| α-helix | 180-182 | 3 | |
| α-helix | 183-190 | 8 | |
| α-helix | 191-193 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 16 | 1 | 4 |
| β-strand | 20 | 1 | 4 |
| β-strand | 24-27 | 4 | 4 |
| α-helix | 28-30 | 3 | |
| α-helix | 33-38 | 6 | |
| α-helix | 41-43 | 3 | |
| α-helix | 47-55 | 9 | |
| β-strand | 61-66 | 6 | 4 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 100-111 | 12 | |
| β-strand | 121-125 | 5 | 4 |
| α-helix | 131-145 | 15 | |
| α-helix | 149-159 | 11 | |
| α-helix | 167-177 | 11 | |
| α-helix | 180-182 | 3 | |
| α-helix | 183-190 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| mRNA capping enzyme | A, B, C, D | protein | 241 | HOMO SAPIENS | O60942 (AlphaFold model) |
>2C46_1 MRNA CAPPING ENZYME (chains A, B, C, D) MHHHHHHSSGVDLGTENLYFQSMAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQ VAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECP TTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQ ARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESETGSSASF G
Crystal Structure of the Human RNA Guanylyltransferase and 5'-Phosphatase. Debreczeni, J., Johansson, C., Longman, E. et al. To be published.
Other PDB entries of the same protein (UniProt O60942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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