Human Complement factor B. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Feb 2007.
Explore 2OK5 in 3D Show helices and sheets RCSB PDB PDBe
2OK5 contains 30 α-helices and 54 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 |
|---|---|---|---|
| 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 | 61 | 1 | 4 |
| β-strand | 67 | 1 | 4 |
| β-strand | 72-75 | 4 | 1 |
| β-strand | 77-78 | 2 | 5 |
| α-helix | 79-81 | 3 | |
| β-strand | 87-90 | 4 | 6 |
| β-strand | 96-97 | 2 | 5 |
| β-strand | 101-106 | 6 | 6 |
| α-helix | 107 | 1 | |
| 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 | 150-152 | 3 | 9 |
| β-strand | 161-165 | 5 | 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 | 202-213 | 12 | |
| β-strand | 215-216 | 2 | 12 |
| β-strand | 234-235 | 2 | 12 |
| β-strand | 243-251 | 9 | 13 |
| α-helix | 258-276 | 19 | |
| β-strand | 283-289 | 7 | 13 |
| β-strand | 293-297 | 5 | 13 |
| α-helix | 307-315 | 9 | |
| β-strand | 328 | 1 | 14 |
| α-helix | 330-341 | 12 | |
| α-helix | 348-349 | 2 | |
| α-helix | 352-354 | 3 | |
| β-strand | 355-363 | 9 | 13 |
| β-strand | 368 | 1 | 14 |
| α-helix | 374-383 | 10 | |
| α-helix | 395-397 | 3 | |
| β-strand | 398-405 | 8 | 13 |
| α-helix | 411-417 | 7 | |
| β-strand | 427-430 | 4 | 13 |
| α-helix | 433-445 | 13 | |
| α-helix | 464-467 | 4 | |
| β-strand | 471-476 | 6 | 15 |
| α-helix | 482-483 | 2 | |
| β-strand | 484-490 | 7 | 15 |
| β-strand | 495-498 | 4 | 15 |
| α-helix | 500-502 | 3 | |
| α-helix | 509-511 | 3 | |
| β-strand | 512-516 | 5 | 15 |
| β-strand | 523 | 1 | 15 |
| β-strand | 525-530 | 6 | 15 |
| β-strand | 553-557 | 5 | 15 |
| β-strand | 564 | 1 | 16 |
| β-strand | 567 | 1 | 16 |
| α-helix | 569-570 | 2 | |
| β-strand | 571 | 1 | 17 |
| α-helix | 572 | 1 | |
| β-strand | 575 | 1 | 18 |
| α-helix | 576-581 | 6 | |
| α-helix | 590-597 | 8 | |
| β-strand | 602-611 | 10 | 17 |
| β-strand | 614-623 | 10 | 17 |
| α-helix | 628-633 | 6 | |
| α-helix | 634-637 | 4 | |
| α-helix | 647-649 | 3 | |
| β-strand | 655-659 | 5 | 17 |
| α-helix | 671-673 | 3 | |
| α-helix | 676 | 1 | |
| β-strand | 677-682 | 6 | 17 |
| β-strand | 685-695 | 11 | 17 |
| α-helix | 700-702 | 3 | |
| β-strand | 714-719 | 6 | 17 |
| α-helix | 720-722 | 3 | |
| α-helix | 724-730 | 7 | |
| β-strand | 738 | 1 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor B | A | protein | 752 | Homo sapiens | P00751 (AlphaFold model) |
>2OK5_1 Complement factor B (chains A) GSHHHHHHGSTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRT CRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGY TLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGL TLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGE QQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYA TYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPE GWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVN QVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPW QAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLF HPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTC QQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEV VTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVP AHARDFHINLFQVLPWLKEKLQDEDLGFLAAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (GOL) are not listed.
Factor B structure provides insights into activation of the central protease of the complement system. Milder, F.J., Gomes, L., Schouten, A. et al. Nat Struct Mol Biol (2007) 14:224-228. DOI 10.1038/nsmb1210 · 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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