Crystal structure of an engineered helicase domain construct for human Bloom syndrome protein (BLM). Determined by X-ray diffraction at 1.53 Å resolution. Released 16 Dec 2020.
Explore 7AUC in 3D Show helices and sheets RCSB PDB PDBe
7AUC contains 28 α-helices and 13 β-strands across 1 chain. 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 | 640-643 | 4 | |
| α-helix | 652-661 | 10 | |
| α-helix | 668-669 | 2 | |
| α-helix | 672-680 | 9 | |
| β-strand | 685-688 | 4 | 1 |
| α-helix | 695-705 | 11 | |
| β-strand | 709-713 | 5 | 1 |
| α-helix | 717-729 | 13 | |
| β-strand | 734-737 | 4 | 1 |
| α-helix | 745-753 | 9 | |
| β-strand | 762-765 | 4 | 1 |
| α-helix | 767-770 | 4 | |
| α-helix | 774-785 | 12 | |
| β-strand | 789-795 | 7 | 1 |
| β-strand | 826-830 | 5 | 1 |
| α-helix | 835-845 | 11 | |
| α-helix | 846-848 | 3 | |
| β-strand | 851-853 | 3 | 1 |
| β-strand | 862-868 | 7 | 2 |
| α-helix | 874-885 | 12 | |
| β-strand | 891-894 | 4 | 2 |
| α-helix | 898-910 | 13 | |
| β-strand | 915-918 | 4 | 2 |
| α-helix | 924-935 | 12 | |
| β-strand | 942-945 | 4 | 2 |
| α-helix | 947-950 | 4 | |
| β-strand | 960-963 | 4 | 2 |
| α-helix | 970-977 | 8 | |
| β-strand | 987-993 | 7 | 2 |
| α-helix | 995-1007 | 13 | |
| α-helix | 1013-1031 | 19 | |
| α-helix | 1037-1044 | 8 | |
| α-helix | 1054-1057 | 4 | |
| α-helix | 1059-1061 | 3 | |
| α-helix | 1064-1067 | 4 | |
| α-helix | 1210-1233 | 24 | |
| α-helix | 1237-1239 | 3 | |
| α-helix | 1243-1252 | 10 | |
| α-helix | 1257-1260 | 4 | |
| α-helix | 1268-1283 | 16 | |
| α-helix | 1286-1288 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bloom syndrome protein,Bloom syndrome protein | A | protein | 562 | Homo sapiens | P54132 (AlphaFold model) |
>7AUC_1 Bloom syndrome protein,Bloom syndrome protein (chains A) MGSAWSHPQFEKSSGLEVLFQGPHMSRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRT NQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL DIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLA RFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRP QVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQR DGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSV EGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYC ENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKGSGGSKALVAKVSQREEMVK KCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGA EVISVLQKYSEWTSPAEDSSPG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| ZN | Zinc ion | Zn | 1 |
| CA | Calcium ion | Ca | 2 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (ACT, EDO, PG4, GOL) are not listed.
Uncovering an allosteric mode of action for a selective inhibitor of human Bloom syndrome protein. Chen, X., Ali, Y.I., Fisher, C.E. et al. Elife (2021) 10. DOI 10.7554/eLife.65339 · PubMed
Other PDB entries of the same protein (UniProt P54132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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