FbaA with Factor H 6-7 domain. Determined by X-ray diffraction at 1.82 Å resolution. Released 4 Feb 2026.
Explore 9MLU in 3D Show helices and sheets RCSB PDB PDBe
9MLU contains 20 α-helices and 30 β-strands across 4 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 | 325 | 1 | 1 |
| β-strand | 333-335 | 3 | 2 |
| α-helix | 338-341 | 4 | |
| α-helix | 342-344 | 3 | |
| β-strand | 347 | 1 | 1 |
| β-strand | 352-357 | 6 | 2 |
| β-strand | 361-362 | 2 | 3 |
| β-strand | 369-375 | 7 | 2 |
| β-strand | 378-380 | 3 | 2 |
| β-strand | 386-387 | 2 | 3 |
| β-strand | 388-390 | 3 | 4 |
| α-helix | 391-393 | 3 | |
| β-strand | 397 | 1 | 5 |
| β-strand | 405-407 | 3 | 4 |
| β-strand | 411-413 | 3 | 6 |
| β-strand | 416 | 1 | 5 |
| α-helix | 417 | 1 | |
| α-helix | 423-425 | 3 | |
| β-strand | 428-432 | 5 | 6 |
| β-strand | 435-437 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 73-86 | 14 | |
| α-helix | 91-103 | 13 | |
| α-helix | 107-113 | 7 | |
| α-helix | 114-118 | 5 | |
| α-helix | 119-122 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 73-86 | 14 | |
| α-helix | 91-103 | 13 | |
| α-helix | 107-112 | 6 | |
| α-helix | 113-118 | 6 | |
| α-helix | 119-123 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor H | A, B | protein | 125 | Homo sapiens | P08603 (AlphaFold model) |
| Fibronectin-binding protein | C, D | protein | 78 | Streptococcus pyogenes | Q93RI1 (AlphaFold model) |
>9MLU_1 Complement factor H (chains A, B) MGTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDG WSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSP TPRCI
>9MLU_2 Fibronectin-binding protein (chains C, D) GPGSNWHHIDKDGLIPLGISLEAAKEEFKKEVEESRLSEAQKETYKQKIKTAPDKDKLLF TYHSEYMTAVKDLPASTE
Structural mechanisms for the recruitment of factor H by Streptococcus pyogenes. Kumar, A., Wang, K.C., Ghosh, P. Structure (2026) 34:778. DOI 10.1016/j.str.2026.02.010 · PubMed
Other PDB entries of the same protein (UniProt P08603 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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