9MMU: M5 protein with Factor H 6-7 domain
M5 protein with Factor H 6-7 domain. Determined by X-ray diffraction at 2.25 Å resolution. Released 4 Feb 2026.
- Method
- X-ray diffraction
- Resolution
- 2.25 Å
- Organisms
- Streptococcus pyogenes str. Manfredo, Homo sapiens
- Chains
- 8
- Atoms
- 4,614
- Mol. weight
- 97.68 kDa
- Released
- 4 Feb 2026
Explore 9MMU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9MMU contains 9 α-helices and 53 β-strands across 8 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.
Chain A: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 103-151 | 49 | |
Chains B and F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 108-152 | 45 | |
Chain C: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 325 | 1 | 1 |
| β-strand | 333-335 | 3 | 2 |
| 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 | 1 | |
| 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 | |
| β-strand | 428-432 | 5 | 6 |
| β-strand | 435-437 | 3 | 6 |
Chain D: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 353-356 | 4 | 7 |
| β-strand | 361-362 | 2 | 8 |
| β-strand | 369-372 | 4 | 7 |
| β-strand | 386-387 | 2 | 8 |
| β-strand | 389-390 | 2 | 9 |
| α-helix | 391 | 1 | |
| β-strand | 397 | 1 | 10 |
| β-strand | 405-406 | 2 | 9 |
| β-strand | 411-413 | 3 | 11 |
| β-strand | 416 | 1 | 10 |
| β-strand | 428-432 | 5 | 11 |
| β-strand | 435-437 | 3 | 11 |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 106-153 | 48 | |
Chain G: 1 helix, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 325 | 1 | 12 |
| β-strand | 333-335 | 3 | 13 |
| β-strand | 347 | 1 | 12 |
| β-strand | 352-357 | 6 | 13 |
| β-strand | 361-362 | 2 | 14 |
| β-strand | 369-375 | 7 | 13 |
| β-strand | 378-380 | 3 | 13 |
| β-strand | 386-387 | 2 | 14 |
| β-strand | 388-390 | 3 | 15 |
| β-strand | 397 | 1 | 16 |
| β-strand | 405-407 | 3 | 15 |
| β-strand | 411-413 | 3 | 17 |
| β-strand | 416 | 1 | 16 |
| α-helix | 417 | 1 | |
| β-strand | 428-432 | 5 | 17 |
| β-strand | 435-437 | 3 | 17 |
Chain H: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 352-356 | 5 | 18 |
| β-strand | 361-362 | 2 | 19 |
| β-strand | 369-373 | 5 | 18 |
| α-helix | 374 | 1 | |
| β-strand | 380 | 1 | 18 |
| β-strand | 386-387 | 2 | 19 |
| β-strand | 390 | 1 | 20 |
| β-strand | 397 | 1 | 21 |
| β-strand | 405 | 1 | 20 |
| β-strand | 411-413 | 3 | 22 |
| β-strand | 416 | 1 | 21 |
| β-strand | 428-432 | 5 | 22 |
| β-strand | 435-437 | 3 | 22 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| M protein, serotype 5 | A, B, E, F | protein | 86 | Streptococcus pyogenes str. Manfredo | P02977 (AlphaFold model) |
| Complement factor H | C, D, G, H | protein | 125 | Homo sapiens | P08603 (AlphaFold model) |
Sequence of entity 1 (A, B, E, F), FASTA
>9MMU_1 M protein, serotype 5 (chains A, B, E, F)
GPGSNEGLKTEKKEHEAENDKLKQQRDTLSTQKETLEREVQNTQYNNETLKIKNGDLTKE
LNKTRQELANKQQESKENEKALNELL
Sequence of entity 2 (C, D, G, H), FASTA
>9MMU_2 Complement factor H (chains C, D, G, H)
MGTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDG
WSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSP
TPRCI
Primary citation
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 P02977 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2KK9 Anti-group A streptococcal vaccine epitope: structure, stability and its ability to…
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