Crystal Structure Analysis of the Bb segment of Factor B complexed with 4-guanidinobenzoic acid. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Dec 2004.
Explore 1RTK in 3D Show helices and sheets RCSB PDB PDBe
1RTK contains 25 α-helices and 23 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 | 244-251 | 8 | 1 |
| α-helix | 258-277 | 20 | |
| β-strand | 283-289 | 7 | 1 |
| β-strand | 293-297 | 5 | 1 |
| α-helix | 302-305 | 4 | |
| α-helix | 307-316 | 10 | |
| α-helix | 319-321 | 3 | |
| α-helix | 330-341 | 12 | |
| α-helix | 352-354 | 3 | |
| β-strand | 356-363 | 8 | 1 |
| α-helix | 374-383 | 10 | |
| α-helix | 395-397 | 3 | |
| β-strand | 398-404 | 7 | 1 |
| α-helix | 411-417 | 7 | |
| β-strand | 427-429 | 3 | 1 |
| α-helix | 433-443 | 11 | |
| α-helix | 446-449 | 4 | |
| α-helix | 464-467 | 4 | |
| β-strand | 471-476 | 6 | 2 |
| β-strand | 484-490 | 7 | 2 |
| β-strand | 495-498 | 4 | 2 |
| α-helix | 500-502 | 3 | |
| α-helix | 509-511 | 3 | |
| β-strand | 512-516 | 5 | 2 |
| β-strand | 523-530 | 8 | 2 |
| α-helix | 540-542 | 3 | |
| β-strand | 553-557 | 5 | 2 |
| β-strand | 564 | 1 | 3 |
| β-strand | 567 | 1 | 3 |
| α-helix | 569-570 | 2 | |
| β-strand | 571 | 1 | 4 |
| β-strand | 575 | 1 | 5 |
| α-helix | 576-581 | 6 | |
| α-helix | 590-597 | 8 | |
| β-strand | 602-611 | 10 | 4 |
| β-strand | 614-623 | 10 | 4 |
| α-helix | 628-633 | 6 | |
| α-helix | 634-637 | 4 | |
| α-helix | 647-649 | 3 | |
| β-strand | 655-659 | 5 | 4 |
| α-helix | 671-673 | 3 | |
| α-helix | 676 | 1 | |
| β-strand | 677-682 | 6 | 4 |
| β-strand | 685-695 | 11 | 4 |
| β-strand | 714-719 | 6 | 4 |
| α-helix | 720-723 | 4 | |
| α-helix | 724-730 | 7 | |
| β-strand | 738 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor B Bb fragment | A | protein | 497 | Homo sapiens | P00751 (AlphaFold model) |
>1RTK_1 Complement factor B Bb fragment (chains A) SMNIYLVLDGSDSIGASNFTGAKKVLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEA DSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILM TDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKD NEQHVCKVKDMECLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKG HESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEA GIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQD IKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVS PYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQ VLPWLKEKLQDEDLGFL
Water and common crystallization additives (IOD, NA) are not listed.
Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase. Ponnuraj, K., Xu, Y., Macon, K. et al. Mol Cell (2004) 14:17-28. DOI 10.1016/S1097-2765(04)00160-1 · 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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