Human Complement Factor B Inhibited by a Slow Off-Rate Modified Aptamer of 31 Bases. Determined by X-ray diffraction at 3.5 Å resolution. Released 9 Dec 2020.
Explore 7JTQ in 3D Show helices and sheets RCSB PDB PDBe
7JTQ contains 50 α-helices and 110 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 | 20 | 1 | 1 |
| β-strand | 23-27 | 5 | 2 |
| α-helix | 28-30 | 3 | |
| β-strand | 32-36 | 5 | 2 |
| β-strand | 41-44 | 4 | 1 |
| β-strand | 48-50 | 3 | 2 |
| β-strand | 51 | 1 | 3 |
| β-strand | 57 | 1 | 3 |
| α-helix | 58-59 | 2 | |
| β-strand | 60 | 1 | 4 |
| β-strand | 68 | 1 | 4 |
| β-strand | 72-75 | 4 | 1 |
| β-strand | 78 | 1 | 5 |
| α-helix | 79-80 | 2 | |
| β-strand | 87-90 | 4 | 6 |
| β-strand | 96 | 1 | 5 |
| β-strand | 101-106 | 6 | 6 |
| β-strand | 111-113 | 3 | 7 |
| β-strand | 117-119 | 3 | 6 |
| β-strand | 120 | 1 | 8 |
| β-strand | 126 | 1 | 8 |
| β-strand | 132-134 | 3 | 7 |
| β-strand | 149-152 | 4 | 9 |
| β-strand | 161-166 | 6 | 9 |
| β-strand | 171-173 | 3 | 10 |
| β-strand | 177-179 | 3 | 9 |
| β-strand | 180 | 1 | 11 |
| β-strand | 186 | 1 | 11 |
| β-strand | 192-194 | 3 | 10 |
| α-helix | 202-210 | 9 | |
| β-strand | 211 | 1 | 12 |
| β-strand | 214 | 1 | 12 |
| β-strand | 215-216 | 2 | 13 |
| β-strand | 234-235 | 2 | 13 |
| β-strand | 243-251 | 9 | 14 |
| α-helix | 255-257 | 3 | |
| α-helix | 262-276 | 15 | |
| α-helix | 282 | 1 | |
| β-strand | 283-289 | 7 | 14 |
| β-strand | 293-297 | 5 | 14 |
| α-helix | 302-304 | 3 | |
| α-helix | 307-314 | 8 | |
| β-strand | 329 | 1 | 15 |
| α-helix | 331-341 | 11 | |
| α-helix | 352-354 | 3 | |
| β-strand | 355-363 | 9 | 14 |
| β-strand | 369 | 1 | 15 |
| α-helix | 374-383 | 10 | |
| α-helix | 395-397 | 3 | |
| β-strand | 398-405 | 8 | 14 |
| α-helix | 411-417 | 7 | |
| β-strand | 427-430 | 4 | 14 |
| α-helix | 433-444 | 12 | |
| α-helix | 445-447 | 3 | |
| β-strand | 471 | 1 | 16 |
| β-strand | 472-476 | 5 | 17 |
| β-strand | 484-486 | 3 | 17 |
| β-strand | 489 | 1 | 16 |
| β-strand | 495-498 | 4 | 16 |
| α-helix | 500-502 | 3 | |
| β-strand | 512-516 | 5 | 17 |
| β-strand | 525-530 | 6 | 16 |
| α-helix | 531 | 1 | |
| β-strand | 553-557 | 5 | 16 |
| β-strand | 571 | 1 | 18 |
| β-strand | 575 | 1 | 19 |
| α-helix | 576-581 | 6 | |
| α-helix | 590-597 | 8 | |
| β-strand | 604-611 | 8 | 18 |
| β-strand | 614-622 | 9 | 18 |
| α-helix | 628-632 | 5 | |
| α-helix | 633-635 | 3 | |
| α-helix | 647-649 | 3 | |
| β-strand | 655-659 | 5 | 18 |
| α-helix | 666-670 | 5 | |
| β-strand | 677-682 | 6 | 18 |
| β-strand | 685-695 | 11 | 18 |
| β-strand | 714-719 | 6 | 18 |
| α-helix | 724-730 | 7 | |
| β-strand | 738 | 1 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor B | A, C | protein | 764 | Homo sapiens | P00751 (AlphaFold model) |
| DNA (32-mer) | B, D | DNA | 32 | synthetic construct |
>7JTQ_1 Complement factor B (chains A, C) MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEY VCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPY YNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQ YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTE TIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKV ASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQ AVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPRE DYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGM VWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVS VGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCT EGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDA QYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWG VVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
>7JTQ_2 DNA (32-MER) (chains B, D) CGCXGAGAAXAGAAGXAGGAGXAXGCXXGCGT
Inhibition of the Complement Alternative Pathway by Chemically Modified DNA Aptamers That Bind with Picomolar Affinity to Factor B. Xu, X., Zhang, C., Denton, D.T. et al. J Immunol (2021) 206:861-873. DOI 10.4049/jimmunol.2001260 · PubMed
Other PDB entries of the same protein (UniProt P00751 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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