human Artemis/SNM1C catalytic domain, crystal form 2. Determined by X-ray diffraction at 2.37 Å resolution. Released 1 Jul 2020.
Explore 6WNL in 3D Show helices and sheets RCSB PDB PDBe
6WNL contains 36 α-helices and 48 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 |
|---|---|---|---|
| β-strand | 15-16 | 2 | 1 |
| α-helix | 21-25 | 5 | |
| β-strand | 29-30 | 2 | 1 |
| α-helix | 36-38 | 3 | |
| α-helix | 45-52 | 8 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 63-71 | 9 | |
| α-helix | 73-81 | 9 | |
| β-strand | 82-84 | 3 | 1 |
| β-strand | 91-96 | 6 | 2 |
| β-strand | 103-112 | 10 | 2 |
| β-strand | 120-125 | 6 | 2 |
| β-strand | 131-133 | 3 | 2 |
| α-helix | 144-146 | 3 | |
| α-helix | 148-150 | 3 | |
| β-strand | 151-152 | 2 | 3 |
| β-strand | 155-156 | 2 | 3 |
| β-strand | 161-164 | 4 | 2 |
| α-helix | 171-173 | 3 | |
| β-strand | 175 | 1 | 4 |
| α-helix | 179-194 | 16 | |
| β-strand | 200-204 | 5 | 5 |
| α-helix | 213-223 | 11 | |
| α-helix | 226 | 1 | |
| β-strand | 227-228 | 2 | 5 |
| α-helix | 233-235 | 3 | |
| α-helix | 239-242 | 4 | |
| β-strand | 245-246 | 2 | 5 |
| β-strand | 253-254 | 2 | 5 |
| α-helix | 261-266 | 6 | |
| β-strand | 276-277 | 2 | 6 |
| β-strand | 280-281 | 2 | 6 |
| α-helix | 282 | 1 | |
| β-strand | 283-290 | 8 | 5 |
| β-strand | 294 | 1 | 4 |
| β-strand | 304-308 | 5 | 5 |
| β-strand | 311-315 | 5 | 5 |
| α-helix | 322-332 | 11 | |
| β-strand | 336-339 | 4 | 2 |
| α-helix | 348-355 | 8 | |
| α-helix | 356-358 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 7 |
| β-strand | 11 | 1 | 7 |
| β-strand | 14-16 | 3 | 8 |
| α-helix | 21-25 | 5 | |
| β-strand | 28-30 | 3 | 8 |
| α-helix | 36-38 | 3 | |
| α-helix | 45-52 | 8 | |
| β-strand | 59-61 | 3 | 8 |
| α-helix | 63-71 | 9 | |
| α-helix | 73-81 | 9 | |
| β-strand | 82-84 | 3 | 8 |
| β-strand | 91-96 | 6 | 9 |
| β-strand | 103-112 | 10 | 9 |
| β-strand | 120-125 | 6 | 9 |
| β-strand | 131-133 | 3 | 9 |
| α-helix | 144-146 | 3 | |
| α-helix | 148-150 | 3 | |
| β-strand | 151-152 | 2 | 10 |
| β-strand | 155-156 | 2 | 10 |
| β-strand | 161-164 | 4 | 9 |
| α-helix | 171-173 | 3 | |
| β-strand | 175 | 1 | 11 |
| α-helix | 179-194 | 16 | |
| β-strand | 200-204 | 5 | 12 |
| α-helix | 213-223 | 11 | |
| α-helix | 226 | 1 | |
| β-strand | 227-228 | 2 | 12 |
| α-helix | 233-235 | 3 | |
| α-helix | 239-242 | 4 | |
| β-strand | 245-246 | 2 | 12 |
| β-strand | 253-254 | 2 | 12 |
| α-helix | 261-266 | 6 | |
| β-strand | 276-277 | 2 | 13 |
| β-strand | 280-281 | 2 | 13 |
| α-helix | 282 | 1 | |
| β-strand | 283-290 | 8 | 12 |
| β-strand | 294 | 1 | 11 |
| β-strand | 304-306 | 3 | 12 |
| β-strand | 311-315 | 5 | 12 |
| α-helix | 322-332 | 11 | |
| β-strand | 336-339 | 4 | 9 |
| α-helix | 348-355 | 8 | |
| α-helix | 356-358 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein artemis | A, B | protein | 375 | Homo sapiens | Q96SD1 (AlphaFold model) |
>6WNL_1 Protein artemis (chains A, B) SSFEGQMAEYPTISIDRFDRENLRARAYFLSHCHKDHMKGLRAPTLKRRLECSLKVYLYC SPVTKELLLTSPKYRFWKKRIISIEIETPTQISLVDEASGEKEEIVVTLLPAGHCPGSVM FLFQGNNGTVLYTGDFRLAQGEAARMELLHSGGRVKDIQSVYLDTTFCDPRFYQIPSREE CLSGVLELVRSWITRSPYHVVWLNCKAAYGYEYLFTNLSEELGVQVHVNKLDMFRNMPEI LHHLTTDRNTQIHACRHPKAEEYFQWSKLPCGITSRNRIPLHIISIKPSTMWFGERSRKT NVIVRTGESSYRACFSFHSSYSEIKDFLSYLCPVNAYPNVIPVGTTMDKVVEILKPLCRS SQSTEPKKGENLYFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Structural analysis of the catalytic domain of Artemis endonuclease/SNM1C reveals distinct structural features. Karim, M.F., Liu, S., Laciak, A.R. et al. J Biol Chem (2020) 295:12368-12377. DOI 10.1074/jbc.RA120.014136 · PubMed
Other PDB entries of the same protein (UniProt Q96SD1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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