Jumonji domain-containing protein 2A with crystallization epitope mutations A91T:T93S. Determined by X-ray diffraction at 1.88 Å resolution. Released 18 Sept 2024.
Explore 9GLE in 3D Show helices and sheets RCSB PDB PDBe
9GLE contains 47 α-helices and 34 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 | 14-15 | 2 | |
| β-strand | 16-18 | 3 | 1 |
| α-helix | 22-25 | 4 | |
| α-helix | 28-37 | 10 | |
| α-helix | 40-43 | 4 | |
| β-strand | 45-48 | 4 | 1 |
| β-strand | 67-68 | 2 | 2 |
| β-strand | 72-79 | 8 | 3 |
| β-strand | 82-89 | 8 | 3 |
| β-strand | 93-94 | 2 | 2 |
| α-helix | 95-103 | 9 | |
| α-helix | 109-111 | 3 | |
| α-helix | 115-125 | 11 | |
| β-strand | 132-133 | 2 | 3 |
| β-strand | 134-138 | 5 | 1 |
| α-helix | 157-160 | 4 | |
| β-strand | 176-180 | 5 | 1 |
| β-strand | 185-189 | 5 | 4 |
| α-helix | 192-194 | 3 | |
| β-strand | 196-204 | 9 | 1 |
| β-strand | 207-212 | 6 | 4 |
| α-helix | 214-216 | 3 | |
| α-helix | 217-227 | 11 | |
| α-helix | 229-234 | 6 | |
| α-helix | 238-241 | 4 | |
| β-strand | 244-246 | 3 | 3 |
| α-helix | 248-253 | 6 | |
| β-strand | 259-263 | 5 | 4 |
| α-helix | 264 | 1 | |
| β-strand | 268-271 | 4 | 1 |
| β-strand | 276-281 | 6 | 4 |
| β-strand | 285-292 | 8 | 1 |
| α-helix | 297-303 | 7 | |
| α-helix | 304-307 | 4 | |
| α-helix | 319-325 | 7 | |
| α-helix | 327-329 | 3 | |
| α-helix | 330-334 | 5 | |
| α-helix | 347-348 | 2 | |
| α-helix | 349-354 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| β-strand | 17-18 | 2 | 5 |
| α-helix | 22-25 | 4 | |
| α-helix | 28-37 | 10 | |
| α-helix | 40-43 | 4 | |
| β-strand | 45-48 | 4 | 5 |
| α-helix | 49-51 | 3 | |
| α-helix | 63-65 | 3 | |
| β-strand | 67-68 | 2 | 6 |
| β-strand | 72-79 | 8 | 7 |
| β-strand | 82-89 | 8 | 7 |
| β-strand | 93-94 | 2 | 6 |
| α-helix | 95-103 | 9 | |
| α-helix | 109-111 | 3 | |
| α-helix | 115-125 | 11 | |
| α-helix | 130-131 | 2 | |
| β-strand | 132-133 | 2 | 7 |
| β-strand | 134-138 | 5 | 5 |
| α-helix | 157-161 | 5 | |
| β-strand | 176-180 | 5 | 5 |
| β-strand | 185-189 | 5 | 8 |
| α-helix | 192-194 | 3 | |
| β-strand | 196-204 | 9 | 5 |
| β-strand | 207-212 | 6 | 8 |
| α-helix | 214-216 | 3 | |
| α-helix | 217-227 | 11 | |
| α-helix | 229-234 | 6 | |
| α-helix | 238-241 | 4 | |
| β-strand | 244-246 | 3 | 7 |
| α-helix | 248-253 | 6 | |
| β-strand | 259-263 | 5 | 8 |
| α-helix | 264 | 1 | |
| β-strand | 268-271 | 4 | 5 |
| β-strand | 276-281 | 6 | 8 |
| β-strand | 285-292 | 8 | 5 |
| α-helix | 297-303 | 7 | |
| α-helix | 304-307 | 4 | |
| α-helix | 319-325 | 7 | |
| α-helix | 327-329 | 3 | |
| α-helix | 330-334 | 5 | |
| α-helix | 347-348 | 2 | |
| α-helix | 349-354 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific demethylase 4A | A, B | protein | 360 | Homo sapiens | O75164 (AlphaFold model) |
>9GLE_1 Lysine-specific demethylase 4A (chains A, B) SMASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASY DDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKTMSVREFRKIANSDKYCTPRYSEFEELER KYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFG MWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLR HKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEY GKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESEL
Water and common crystallization additives (EDO, SO4) are not listed.
A fast, parallel method for efficiently exploring crystallization behaviour of large numbers of protein variants. Fairhead, M., Strain-Damerell, C., Ye, M. et al. To be published.
Other PDB entries of the same protein (UniProt O75164 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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